Protein Complex accession Recommended name Aliases for complex Identifiers (and stoichiometry) of molecules in complex Confidence Experimental evidence Description Complex properties Complex assembly P00363 CPX-1967 Plasma membrane fumarate reductase complex QFR complex|quinol-fumarate reductase respiratory complex|fumarate reductase complex CHEBI:17594(2)|CHEBI:16238(1)|CHEBI:33725(1)|CHEBI:47402(1)|CHEBI:33739(1)|P00363(1)|P0AC47(1)|P0A8Q3(1)|P0A8Q0(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-1033003 Catalyzes the terminal step of anaerobic respiration. Electrons are donated to membrane-bound subunits FrdC and FrdD by 2 quinol (hydroquinone) molecules and transferred to a flavin adenine nucleotide (FAD, covalently-bound to subunit FrdA) through three distinct Fe-S clusters (within subunit FrdB). Ultimately, the electrons are used to reduce FAD-bound fumarate to succinate. Electrons can also be transported in the opposite direction where they are donated by succinate and ultimately reduce quinone to quinol. Member of the Complex II family. The functionally inverse complex found in aerobic respiration is the SQR complex (CPX-1931). QFR is composed of a FAD-binding catalytic subunit FrdA, a Fe-S cluster-containing electron transfer subunit FrdB and the transmembrane subunits FrdC and FrdD. Fumarate binds to the FrdA-bound FAD cofactor and the quinol molecules bind to 2 binding sites in the FrdC-FrdD dimer interface. FrdA and FrdB comprise the cytoplasmic, soluble, subunits of the complex, whereas FrdC and FrdD make up the hydrophobic, transmembrane subunits. Heterotetramer P00370 CPX-1976 Glutamate dehydrogenase complex NADP+-dependent glutamate dehydrogenase|glutamate dehydrogenase (NADP+)|L-glutamate dehydrogenase|L-glutamic acid dehydrogenase|NAD(P)-glutamate dehydrogenase|NAD(P)H-dependent glutamate dehydrogenase|dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate))|glutamic acid dehydrogenase|glutamic dehydrogenase|L-glutamate:NADP+ oxidoreductase (deaminating)|Dhe4 complex P00370(1)|P00370(1)|P00370(1)|P00370(1)|P00370(1)|CHEBI:18009(1)|P00370(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-6896131 Catalyses the reversible oxidative deamination of L-glutamate to alpha-ketoglutarate using NADH+ as cofactor. Is the beta subunit of the glutamate synthase. Links amino acid metabolism to the tricarboxylic acid (TCA) cycle. NADP+ cofactor binds to only one subunit of the enzyme. Homohexamer P00370 CPX-1976 Glutamate dehydrogenase complex NADP+-dependent glutamate dehydrogenase|glutamate dehydrogenase (NADP+)|L-glutamate dehydrogenase|L-glutamic acid dehydrogenase|NAD(P)-glutamate dehydrogenase|NAD(P)H-dependent glutamate dehydrogenase|dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate))|glutamic acid dehydrogenase|glutamic dehydrogenase|L-glutamate:NADP+ oxidoreductase (deaminating)|Dhe4 complex P00370(1)|P00370(1)|P00370(1)|P00370(1)|P00370(1)|CHEBI:18009(1)|P00370(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-6896131 Catalyses the reversible oxidative deamination of L-glutamate to alpha-ketoglutarate using NADH+ as cofactor. Is the beta subunit of the glutamate synthase. Links amino acid metabolism to the tricarboxylic acid (TCA) cycle. NADP+ cofactor binds to only one subunit of the enzyme. Homohexamer P00370 CPX-1976 Glutamate dehydrogenase complex NADP+-dependent glutamate dehydrogenase|glutamate dehydrogenase (NADP+)|L-glutamate dehydrogenase|L-glutamic acid dehydrogenase|NAD(P)-glutamate dehydrogenase|NAD(P)H-dependent glutamate dehydrogenase|dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate))|glutamic acid dehydrogenase|glutamic dehydrogenase|L-glutamate:NADP+ oxidoreductase (deaminating)|Dhe4 complex P00370(1)|P00370(1)|P00370(1)|P00370(1)|P00370(1)|CHEBI:18009(1)|P00370(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-6896131 Catalyses the reversible oxidative deamination of L-glutamate to alpha-ketoglutarate using NADH+ as cofactor. Is the beta subunit of the glutamate synthase. Links amino acid metabolism to the tricarboxylic acid (TCA) cycle. NADP+ cofactor binds to only one subunit of the enzyme. Homohexamer P00370 CPX-1976 Glutamate dehydrogenase complex NADP+-dependent glutamate dehydrogenase|glutamate dehydrogenase (NADP+)|L-glutamate dehydrogenase|L-glutamic acid dehydrogenase|NAD(P)-glutamate dehydrogenase|NAD(P)H-dependent glutamate dehydrogenase|dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate))|glutamic acid dehydrogenase|glutamic dehydrogenase|L-glutamate:NADP+ oxidoreductase (deaminating)|Dhe4 complex P00370(1)|P00370(1)|P00370(1)|P00370(1)|P00370(1)|CHEBI:18009(1)|P00370(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-6896131 Catalyses the reversible oxidative deamination of L-glutamate to alpha-ketoglutarate using NADH+ as cofactor. Is the beta subunit of the glutamate synthase. Links amino acid metabolism to the tricarboxylic acid (TCA) cycle. NADP+ cofactor binds to only one subunit of the enzyme. Homohexamer P00370 CPX-1976 Glutamate dehydrogenase complex NADP+-dependent glutamate dehydrogenase|glutamate dehydrogenase (NADP+)|L-glutamate dehydrogenase|L-glutamic acid dehydrogenase|NAD(P)-glutamate dehydrogenase|NAD(P)H-dependent glutamate dehydrogenase|dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate))|glutamic acid dehydrogenase|glutamic dehydrogenase|L-glutamate:NADP+ oxidoreductase (deaminating)|Dhe4 complex P00370(1)|P00370(1)|P00370(1)|P00370(1)|P00370(1)|CHEBI:18009(1)|P00370(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-6896131 Catalyses the reversible oxidative deamination of L-glutamate to alpha-ketoglutarate using NADH+ as cofactor. Is the beta subunit of the glutamate synthase. Links amino acid metabolism to the tricarboxylic acid (TCA) cycle. NADP+ cofactor binds to only one subunit of the enzyme. Homohexamer P00370 CPX-1976 Glutamate dehydrogenase complex NADP+-dependent glutamate dehydrogenase|glutamate dehydrogenase (NADP+)|L-glutamate dehydrogenase|L-glutamic acid dehydrogenase|NAD(P)-glutamate dehydrogenase|NAD(P)H-dependent glutamate dehydrogenase|dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate))|glutamic acid dehydrogenase|glutamic dehydrogenase|L-glutamate:NADP+ oxidoreductase (deaminating)|Dhe4 complex P00370(1)|P00370(1)|P00370(1)|P00370(1)|P00370(1)|CHEBI:18009(1)|P00370(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-6896131 Catalyses the reversible oxidative deamination of L-glutamate to alpha-ketoglutarate using NADH+ as cofactor. Is the beta subunit of the glutamate synthase. Links amino acid metabolism to the tricarboxylic acid (TCA) cycle. NADP+ cofactor binds to only one subunit of the enzyme. Homohexamer P00968 CPX-1937 Carbamoyl phosphate synthetase complex Carbamoyl phosphate synthetase complex|CPS P0A6F1(4)|P00968(4) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-1026932 Plays a key role in both pyrimidine and arginine biosynthesis by catalyzing the production of carbamoyl phosphate from one molecule of bicarbonate, two molecules of MgATP, and one molecule of glutamine. Consists of two polypeptide chains referred to as the small and large subunits, which contain a total of three separate active sites that are connected by an intramolecular tunnel. The small subunit harbors one of these active sites and is responsible for the hydrolysis of glutamine to glutamate and ammonia. The large subunit binds the two required molecules of MgATP and is involved in assembling the final product. Compounds such as L-ornithine, UMP, and IMP allosterically regulate the enzyme. - Heterooctamer P02359 CPX-3802 30S small ribosomal subunit 30S subunit P68679(1)|URS00005CADE5_83333(1)|P0A7R5(1)|P0A7X3(1)|P0A7T3(1)|P0A7U3(1)|P0A7U7(1)|P0A7V3(1)|P0A7R9(1)|P0A7W7(1)|P0A7T7(1)|P0AG63(1)|P0A7V0(1)|P0ADZ4(1)|P0A7S3(1)|P0A7V8(1)|P0A7W1(1)|P0A7S9(1)|P02359(1)|P0AG67(1)|P02358(1)|P0AG59(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit (CPX-3807) which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 50S subunit acts as the decoding centre of the ribosome which brings mRNA and aminoacylated transfer (t)RNAs together, with the 16S ribosomal (r)RNA being required for the selection of the cognate tRNA. Guides the initiating start codon AUG of mRNA into position by recognizing the Shine-Dalgarno sequence, a complementary binding site about 8 base pairs upstream from the start codon. In order to form the translation complex with the 50S subunit, the 30S subunit must bind the Translation Initiation factor complex (CPX-2244), mRNA, and f-met-tRNA. The mRNA entrance channel is formed mainly by proteins rpsC, rpsD, and rpsE. Hetero22-mer P05055 CPX-403 Degradosome RNA degradosome - core component|RNA degradosome|Degradosome P21513(12)|P0A6P9(16)|P05055(12)|P0A8J8(8) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-849044 Key role in mRNA degradation and RNA processing. RNA binds to RnaE, RhlB helicase is necessary to unwind the RNA secondary structures and, once unwound, the 3â€?5â€?decay of the transcripts is ensued by phosphate-dependent PNPase. RNase E bound-enolase may connect cellular metabolic status with post-transcriptional gene regulation and link RNA degradation to glycolytic processes. A dynamic set of minor components of this complex may regulate its function and compartmentalization. Structured as ordered helical elements arranged in a coil. RNase E provides the backbone of the complex and the N-terminus of this enzyme tethers the degradosome to the cytoplasmic membrane. A ratio of four PNPase trimers binds to three RNase E tetramers and eight enolase dimers and eight RhlB helicase N-terminal domains bind to the C-terminal tails of RNase E. Mg2+ ions coordinate the N-terminal domains of RNase E into catalytic tetrameric domains. - P06959 CPX-3943 Pyruvate dehydrogenase complex PDH complex|dihydrolipoyl dehydrogenase complex|PDHC P0A9P0(12)|P0AFG8(24)|P06959(24)|CHEBI:57692(12)|CHEBI:83088(0)|CHEBI:58937(0)|CHEBI:18420(0) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Converts pyruvate to acetyl-CoA and CO2, thus providing a metabolic connection between glycolysis, whose end product is pyruvate, and the tricarboxylic acid cycle, which starts with acetyl-CoA. It contains multiple copies of three enzymatic components, that are encoded by a single operon: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). In anaerobic Escherichia coli, the complex is normally inactive due to inhibition of ldpA by NADH. During aerobic growth, the NADH generated in glycolysis is oxidized and the complex becomes active. Assembled symmetrically around a 24-polypeptide structural core with octahedral symmetry built mainly from catalytic domains in the aceF components, with the peripheral aceE and lpdA components displaced and separated from the core by large distances but tethered to it by flexible linkers non-covalently bound to them. - P07363 CPX-1077 Chemotaxis phosphorelay complex CheA-CheY - CHEBI:18420(1)|P0AE67(1)|P07363(1) ECO:0000353(physical interaction evidence used in manual assertion) - Plays a role in chemotaxis, the movement toward or away from chemicals. The complex is formed to activate cheY protein that then induces the change of the flagellar rotors from counterclocwise to clockwise rotation. cheA interacts with transmembrane chemoreceptors to generate stimulus signals via autophosphorylion of cheA which then serves as a phosphodonor for cheY. The P-cheY generated by this interaction binds to fliM (P06974), the switch component of the flagellar motor. - Heterodimer P09152 CPX-1974 Nitrate reductase A complex Nar complex|NarGHI complex|dissimilatory nitrate reductase|cytoplasmic membrane-bound quinol-nitrate oxidoreductase CHEBI:60539(1)|CHEBI:49883(1)|CHEBI:21137(1)|CHEBI:21137(1)|CHEBI:60539(1)|CHEBI:49883(1)|P11349(1)|P11350(1)|CHEBI:30413(2)|CHEBI:49883(3)|P09152(1)|P11350(1)|P11349(1)|P09152(1)|CHEBI:49883(3)|CHEBI:30413(2) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-1037008 Involved in electron transport during anaerobic respiration: electrons are passed from the formate dehydrogenase-N (Fdh-N) complex (CPX-1975) to nitrate reductase (NarGHI) complex via a quinone-quinol redox reaction. Within NarGHI, the distal heme molecule of NarI receives electrons from quinol (hydroquinone), passes them on to the proximal heme which passes it down a Fe-S cluster chain to the molybdopterin cofactor Mo-bisMGD where they reduce nitrate to nitrite. The collaboration of these two complexes contributes to the proton motive force: electrons are ultimately donated to Fdh-N by formate in the periplasm, transported to the cytoplasm and accepted by nitrate. Hydrogen ions are transported in the opposite direction: Quinone is reduced to quinol by cytoplasmic protons which are in turn released into the periplasm when quinol is oxidized to quinone. Dimeric heterotrimer. MW = ~ 500 kD (hexamer). NarGHI is composed of a Mo-bisMGD-containing catalytic subunit NarG, a Fe-S cluster-containing electron transfer subunit NarH and a heme-containing membrane anchor subunit NarI. Quinol binds to the 'Q-Site' of the heme-containing NarI subunit and nitrate to the NarG-bound Mo-bisMGD cofactor. NarGH (NarG-NarH) forms the cytoplasmic part of the enzyme and is chaperoned to the transmembrane subunit NarI by NarJ (P0AF26). NarI anchors NarGH to the cytoplasmic side of the membrane. Heterohexamer P09152 CPX-1974 Nitrate reductase A complex Nar complex|NarGHI complex|dissimilatory nitrate reductase|cytoplasmic membrane-bound quinol-nitrate oxidoreductase CHEBI:60539(1)|CHEBI:49883(1)|CHEBI:21137(1)|CHEBI:21137(1)|CHEBI:60539(1)|CHEBI:49883(1)|P11349(1)|P11350(1)|CHEBI:30413(2)|CHEBI:49883(3)|P09152(1)|P11350(1)|P11349(1)|P09152(1)|CHEBI:49883(3)|CHEBI:30413(2) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-1037008 Involved in electron transport during anaerobic respiration: electrons are passed from the formate dehydrogenase-N (Fdh-N) complex (CPX-1975) to nitrate reductase (NarGHI) complex via a quinone-quinol redox reaction. Within NarGHI, the distal heme molecule of NarI receives electrons from quinol (hydroquinone), passes them on to the proximal heme which passes it down a Fe-S cluster chain to the molybdopterin cofactor Mo-bisMGD where they reduce nitrate to nitrite. The collaboration of these two complexes contributes to the proton motive force: electrons are ultimately donated to Fdh-N by formate in the periplasm, transported to the cytoplasm and accepted by nitrate. Hydrogen ions are transported in the opposite direction: Quinone is reduced to quinol by cytoplasmic protons which are in turn released into the periplasm when quinol is oxidized to quinone. Dimeric heterotrimer. MW = ~ 500 kD (hexamer). NarGHI is composed of a Mo-bisMGD-containing catalytic subunit NarG, a Fe-S cluster-containing electron transfer subunit NarH and a heme-containing membrane anchor subunit NarI. Quinol binds to the 'Q-Site' of the heme-containing NarI subunit and nitrate to the NarG-bound Mo-bisMGD cofactor. NarGH (NarG-NarH) forms the cytoplasmic part of the enzyme and is chaperoned to the transmembrane subunit NarI by NarJ (P0AF26). NarI anchors NarGH to the cytoplasmic side of the membrane. Heterohexamer P0A6B7 CPX-2139 IscS-TusA complex - P0A6B7(1)|P0A890(1)|P0A890(1)|P0A6B7(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-15849970 Involved in the sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm5s2U) at tRNA wobble positions. TusA stimulates IscS activity while IscS transfers sulfur on Cys19-TusA in a transpersulfidation reaction. In turn, TusA transfers the sulfur to TusD in the TusA-TusBCD-TusE-MnmA pathway. Heterotetramer, consisting of a central IscS dimer (CPX-2136) with the TusA protomers bound to one of the IscS units each via a persulfide (-SSH) group binding Cys328-IscS and Cys19-TusA. Heterotetramer P0A6B7 CPX-2139 IscS-TusA complex - P0A6B7(1)|P0A890(1)|P0A890(1)|P0A6B7(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-15849970 Involved in the sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm5s2U) at tRNA wobble positions. TusA stimulates IscS activity while IscS transfers sulfur on Cys19-TusA in a transpersulfidation reaction. In turn, TusA transfers the sulfur to TusD in the TusA-TusBCD-TusE-MnmA pathway. Heterotetramer, consisting of a central IscS dimer (CPX-2136) with the TusA protomers bound to one of the IscS units each via a persulfide (-SSH) group binding Cys328-IscS and Cys19-TusA. Heterotetramer P0A6B7 CPX-2136 L-cysteine desulfurase complex cysteine desulfurase|cysteine desulfurylase|L-cysteine:acceptor sulfurtransferase P0A6B7(2) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-8851899 An L-cysteine desulfurase complex that catalyses L-cysteine or selenocysteine to L-alanine and either atomic sulfur, as sulfane or (per)sulfide (under reducing conditions) group, or selenium, respectively. The desulfurase activity of IscS is activated by interaction of partner proteins to form a persulfide adduct of Cys328. By changing binding partners, IscS selects the sulfur flow through various sulfur trafficking pathways in the cell It provides the sulfur moiety for a variety of pathways such as iron-sulfur cluster formation, e.g. on apo-protein IscU (P0ACD4), for transpersulfidation reactions, e.g. thiol-group formation on Cys456-ThiF (P30138) during thiamine pyrophospate biosynthesis and for biosynthesis pathways of nicotinic acids, biotin or molybdopterin (via MoeB-MoaD complex, CPX-1968). It is a master enzyme responsible for biosynthesis of all thio-containing RNA modifications (e.g. via ThiL [CPX-2140], TusA-TusBCD-TusE cascade [CPX-2139], IscU [CPX-2141]). It delivers selenium in the pathway for the biosynthesis of selenophosphate. Homodimer. Consists of 2 domains: a small domain (aa1-15, aa264-404) containing the sulfur-accepting Cys-328, and a large domain (aa16-263) harbouring the dimerisation site, the PLP cofactor (bound to Lys-206) and the cysteine substrate-binding pocket. Homodimer P0A6B7 CPX-2141 IscS-IscU complex - P0ACD4(2)|P0A6B7(2) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-15850249 Involved in the sulfur transfer during iron-sulfur cluster assembly and in the modification of tRNA wobble positions. IscS desulfurases L-cysteine and transfers sulfur on IscU while the latter is in the D-state, a partly disordered state that contains an ordered domain that stabilizes two cis peptidyl–prolyl peptide bonds. After Fe-S cluster formation on IscU, IscU converts to the S-state, which has a lower affinity for IscS and minimizes product inhibition. Heterotetramer, consisting of a central IscS dimer with the IscU protomers attached to one of the IscS units each via a disulfide (-SSH) group on Cys328-IscS. Heterotetramer P0A6B7 CPX-2140 IscS-ThiL complex - P0AGG0(0)|P0A6B7(0) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-15850110 IscS desulfurases L-cysteine and transfers the sulfur moiety to Cys456 on ThiI in a transpersulfidation reaction. Downstream, ThiL is involved in thiamine-pyrophosphate biosynthesis, the active form of vitamin B1. IscS and ThiL are probably bound to each other via a persulfide (-SSH) group binding Cys328-IscS and Cys456-ThiL. - P0A6F5 CPX-2113 GroEL-GroES complex GroEL/ES chaperonin system|CH10-CH60 complex P0A6F5(14)|P0A6F9(7) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-1039873 Member of the chaperonin class of molecular chaperones required for the ATP-driven assisted folding of many proteins. Direct contact between substrate proteins and the C-terminal tails of the GroEL subunits helps prevent premature substrate protein escape during encapsulation. Encapsulation seals the GroEL cavity and results in the release of the substrate protein into an enlarged GroEL-GroES chamber. Protein folding is initiated by a conformational shift within the GroEL-GroES complex. Hydrolysis of ATP and binding of a new substrate protein to the opposite cavity sends an allosteric signal causing GroES and the encapsulated protein to be released into the cytosol. GroEL is a tetradecamer of 57 kDa subunits, arranged as two stacked, seven-membered rings, each containing a large, solvent-filled cavity. The cavity-facing surface of the apical domain of each subunit is lined with hydrophobic amino acids that tightly bind substrates. Efficient folding of proteins requires encapsulation of the nonnative substrate protein within a cavity formed by GroEL plus the smaller, ring-shaped, heptameric cochaperonin GroES. MW = 57 kD (monomer) 21-mer P0A6F9 CPX-2113 GroEL-GroES complex GroEL/ES chaperonin system|CH10-CH60 complex P0A6F5(14)|P0A6F9(7) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-1039873 Member of the chaperonin class of molecular chaperones required for the ATP-driven assisted folding of many proteins. Direct contact between substrate proteins and the C-terminal tails of the GroEL subunits helps prevent premature substrate protein escape during encapsulation. Encapsulation seals the GroEL cavity and results in the release of the substrate protein into an enlarged GroEL-GroES chamber. Protein folding is initiated by a conformational shift within the GroEL-GroES complex. Hydrolysis of ATP and binding of a new substrate protein to the opposite cavity sends an allosteric signal causing GroES and the encapsulated protein to be released into the cytosol. GroEL is a tetradecamer of 57 kDa subunits, arranged as two stacked, seven-membered rings, each containing a large, solvent-filled cavity. The cavity-facing surface of the apical domain of each subunit is lined with hydrophobic amino acids that tightly bind substrates. Efficient folding of proteins requires encapsulation of the nonnative substrate protein within a cavity formed by GroEL plus the smaller, ring-shaped, heptameric cochaperonin GroES. MW = 57 kD (monomer) 21-mer P0A6H1 CPX-3176 Endopeptidase ClpXP complex ClpXP protease complex P0A6H1(6)|P0A6G7(7)|P0A6G7(7)|P0A6H1(6) ECO:0005546(biological system reconstruction evidence based on paralogy evidence used in manual assertion) - ATP-dependent serine protease which degrades intracellular unfolded or misfolded proteins. ClpX assembles into hexameric rings that bind coaxially to the ClpP tetradecamer (CPX-3178) forming a barrel-like holoenzyme complex. The six Ile-Gly-Phe loops of a ClpX hexamer dock in the hydrophobic pockets located near the outer edge of the apical surface of each ClpP heptameric ring. Binding of these hexameric ATPases to the ClpP tetradecamer mediates unfolding of substrates in an ATP-dependent manner. The unfolded polypeptide is threaded into the ClpP inner chamber through the axial channel and degraded. 26-mer P0A6H1 CPX-3176 Endopeptidase ClpXP complex ClpXP protease complex P0A6H1(6)|P0A6G7(7)|P0A6G7(7)|P0A6H1(6) ECO:0005546(biological system reconstruction evidence based on paralogy evidence used in manual assertion) - ATP-dependent serine protease which degrades intracellular unfolded or misfolded proteins. ClpX assembles into hexameric rings that bind coaxially to the ClpP tetradecamer (CPX-3178) forming a barrel-like holoenzyme complex. The six Ile-Gly-Phe loops of a ClpX hexamer dock in the hydrophobic pockets located near the outer edge of the apical surface of each ClpP heptameric ring. Binding of these hexameric ATPases to the ClpP tetradecamer mediates unfolding of substrates in an ATP-dependent manner. The unfolded polypeptide is threaded into the ClpP inner chamber through the axial channel and degraded. 26-mer P0A6H5 CPX-2104 HslUV protease complex HslU—HslV peptidase|HslU-HslV complex|protease-associated ATPase|ClpQ|ClpYQ|ClpYQ protease|HslUV|HslV-HslU|HslV peptidase|ATP-dependent HslV-HslU proteinase|caseinolytic protease X|caseinolytic proteinase X|ClpXP ATP-dependent protease|ClpXP protease|ClpXP serine proteinase|Escherichia coli ClpXP serine proteinase|HslUV protease|HslUV proteinase|HslVU protease|HslVU proteinase|protease ClpYQ|protease CodWX|protease HslVU|proteinase ClpYQ|proteinase HslUV P0A7B8(12)|P0A6H5(6) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-8754615 A proteasome-like degradation complex with two functional subunits: the HslU hexamer forms the ATPase subunit which has chaperone activity and the HslV duodecamer forms the protease subunit. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. ATP hydrolysis causes a conformational change in the HslU subunit 'closing' the central pore and 'un-docking' the ATPase unit from the protease by way of flicking the HslU C-terminus from the HslV-HslV interface into the HslU-HslU interface. The complex has been shown to be involved in the specific degradation of heat shock induced transcription factors such as RpoH and SulA. In addition, small hydrophobic peptides are also hydrolyzed by HslV. HslV has weak protease activity even in the absence of HslU, but this activity is induced more than 100-fold in the presence of HslU. Owing to the size of the central pore of both subunits HslV is not believed to degrade folded proteins. hetero-octadecamer, consisting of the ring-shaped, homo-hexameric ATPase subunit HslU with chaperon activity and the ringshaped, double-homo-hexameric protease subunit HslV. There are either 3 or 6 ADPs attached to the complex. A second HslU hexamer may attach to the other side of the HslV subunit but the x-ray structures are not clear regarding this extension to the complex. Hetero-octadecamer P0A6P9 CPX-403 Degradosome RNA degradosome - core component|RNA degradosome|Degradosome P21513(12)|P0A6P9(16)|P05055(12)|P0A8J8(8) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-849044 Key role in mRNA degradation and RNA processing. RNA binds to RnaE, RhlB helicase is necessary to unwind the RNA secondary structures and, once unwound, the 3â€?5â€?decay of the transcripts is ensued by phosphate-dependent PNPase. RNase E bound-enolase may connect cellular metabolic status with post-transcriptional gene regulation and link RNA degradation to glycolytic processes. A dynamic set of minor components of this complex may regulate its function and compartmentalization. Structured as ordered helical elements arranged in a coil. RNase E provides the backbone of the complex and the N-terminus of this enzyme tethers the degradosome to the cytoplasmic membrane. A ratio of four PNPase trimers binds to three RNase E tetramers and eight enolase dimers and eight RhlB helicase N-terminal domains bind to the C-terminal tails of RNase E. Mg2+ ions coordinate the N-terminal domains of RNase E into catalytic tetrameric domains. - P0A6T9 CPX-3949 Glycine cleavage system complex Gycine decarboxylase complex|Glycine cleavage complex|gcvP/T/L/H complex P0A9P0(0)|P27248(0)|P0A6T9(0)|P33195(0)|CHEBI:597326(0)|CHEBI:57692(0)|CHEBI:83088(0) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Multienzyme complex that catalyses the reversible oxidation of glycine, yielding carbon dioxide (CO), ammonia (NH3), 5,10-methylenetetrahydrofolate and a reduced pyridine nucleotide. The 1-carbon units thus generated are used in the synthesis of purines, histidine, thymine, pantothenate, and methionine and in the formylation of the aminoacylated initiator fMet-TRNAfMet required for translation initiation. gcvP binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO2 is released and the remaining methylamine moiety is transferred to the lipoamide cofactor of gcvH, which is bound to the P protein prior to decarboxylation of glycine. gcvT catalyzes the release of NH3 from the methylamine group and transfers the remaining C1 unit to tetrahydrofolate, forming 5,10-methylenetetrahydrofolate. lpdA then oxidizes the lipoic acid component of the H protein and transfers the electrons to NAD+, to form NADH . - - P0A6X7 CPX-1957 IHF complex integration host factor complex|integration host factor-DNA complex|IHF-DNA complex P0A6Y1(1)|P0A6X7(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-6675531 Histone-like, specific DNA-binding complex that functions in genetic recombination as well as in transcriptional and translational control. DNA-binding is both, topology- or structural-dependent and sequence-specific. Heterodimer that binds to double-stranded DNA. Heterodimer P0A6Y1 CPX-1957 IHF complex integration host factor complex|integration host factor-DNA complex|IHF-DNA complex P0A6Y1(1)|P0A6X7(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-6675531 Histone-like, specific DNA-binding complex that functions in genetic recombination as well as in transcriptional and translational control. DNA-binding is both, topology- or structural-dependent and sequence-specific. Heterodimer that binds to double-stranded DNA. Heterodimer P0A705 CPX-2244 Translation initiation factor complex 30S ribosomal translation pre-initiation complex P0A707(0)|P0A705(1)|P69222(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Required for initiation of protein synthesis, when the ribosome recruits an mRNA for translation and establishes the reading frame by binding initiator tRNA to the start codon in the P site of the small (30S) ribosomal subunit (CPX-3802). Assembles on the 30S subunit to form a transient 30S preinitiation complex (PIC). IF3 and IF2 are the first factors to arrive, forming an unstable 30S–IF2–IF3 complex. Subsequently, IF1 joins and locks the factors in a kinetically stable 30S PIC to which fMet-tRNAfMet is recruited. The complex dissociates on binding of the 50S ribosomal subunit. - - P0A707 CPX-2244 Translation initiation factor complex 30S ribosomal translation pre-initiation complex P0A707(0)|P0A705(1)|P69222(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Required for initiation of protein synthesis, when the ribosome recruits an mRNA for translation and establishes the reading frame by binding initiator tRNA to the start codon in the P site of the small (30S) ribosomal subunit (CPX-3802). Assembles on the 30S subunit to form a transient 30S preinitiation complex (PIC). IF3 and IF2 are the first factors to arrive, forming an unstable 30S–IF2–IF3 complex. Subsequently, IF1 joins and locks the factors in a kinetically stable 30S PIC to which fMet-tRNAfMet is recruited. The complex dissociates on binding of the 50S ribosomal subunit. - - P0A7F3 CPX-3091 Aspartate carbamoyltransferase complex ATCase|aspartate transcarbamylase P0A786(1)|P0A786(1)|P0A786(1)|P0A786(1)|P0A7F3(2)|P0A7F3(2)|P0A7F3(2)|CHEBI:29105(2)|CHEBI:29105(2)|CHEBI:29105(2)|P0A786(1)|P0A786(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-1039664 Catalyzes the committed step in pyrimidine nucleotide biosynthesis and allosterically regulates the pathway. The enzyme is activated by ATP, inhibited by CTP and can be further inhibited by UTP, although UTP alone has little effect on activity. The catalytic mechanism is ordered, Carbamoyl phosphate binds before aspartate and carbamoyl aspartate leaves before phosphate. Mol. wt = 310 kDa. The six regulatory chains and six catalytic chains arranged into three regulatory dimers and two catalytic trimers. Each regulatory chain is composed of two separate folding domains, the allosteric domain, responsible for binding the nucleotide effectors, and the zinc domain, responsible for the binding of a structural zinc ion. Displays cooperative kinetic properties with the enzyme in a dynamic equilibrium between a low-activity, low-affinity T state and a high-activity, high-affinity R state. Heterododecamer P0A7F3 CPX-3091 Aspartate carbamoyltransferase complex ATCase|aspartate transcarbamylase P0A786(1)|P0A786(1)|P0A786(1)|P0A786(1)|P0A7F3(2)|P0A7F3(2)|P0A7F3(2)|CHEBI:29105(2)|CHEBI:29105(2)|CHEBI:29105(2)|P0A786(1)|P0A786(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-1039664 Catalyzes the committed step in pyrimidine nucleotide biosynthesis and allosterically regulates the pathway. The enzyme is activated by ATP, inhibited by CTP and can be further inhibited by UTP, although UTP alone has little effect on activity. The catalytic mechanism is ordered, Carbamoyl phosphate binds before aspartate and carbamoyl aspartate leaves before phosphate. Mol. wt = 310 kDa. The six regulatory chains and six catalytic chains arranged into three regulatory dimers and two catalytic trimers. Each regulatory chain is composed of two separate folding domains, the allosteric domain, responsible for binding the nucleotide effectors, and the zinc domain, responsible for the binding of a structural zinc ion. Displays cooperative kinetic properties with the enzyme in a dynamic equilibrium between a low-activity, low-affinity T state and a high-activity, high-affinity R state. Heterododecamer P0A7F3 CPX-3091 Aspartate carbamoyltransferase complex ATCase|aspartate transcarbamylase P0A786(1)|P0A786(1)|P0A786(1)|P0A786(1)|P0A7F3(2)|P0A7F3(2)|P0A7F3(2)|CHEBI:29105(2)|CHEBI:29105(2)|CHEBI:29105(2)|P0A786(1)|P0A786(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-1039664 Catalyzes the committed step in pyrimidine nucleotide biosynthesis and allosterically regulates the pathway. The enzyme is activated by ATP, inhibited by CTP and can be further inhibited by UTP, although UTP alone has little effect on activity. The catalytic mechanism is ordered, Carbamoyl phosphate binds before aspartate and carbamoyl aspartate leaves before phosphate. Mol. wt = 310 kDa. The six regulatory chains and six catalytic chains arranged into three regulatory dimers and two catalytic trimers. Each regulatory chain is composed of two separate folding domains, the allosteric domain, responsible for binding the nucleotide effectors, and the zinc domain, responsible for the binding of a structural zinc ion. Displays cooperative kinetic properties with the enzyme in a dynamic equilibrium between a low-activity, low-affinity T state and a high-activity, high-affinity R state. Heterododecamer P0A7J3 CPX-3807 50S large ribosomal subunit 50S subunit P0A7P5(1)|P0A7N1(1)|URS000002D309_83333(1)|URS00005B2216_83333(1)|P0A7Q6(1)|P02413(1)|P0A7Q1(1)|P0AG48(1)|P0AG51(1)|P0AG44(1)|P0AA10(1)|P0A7R1(1)|P0A7M2(1)|P0C018(1)|P0A7N4(1)|P0A7M6(1)|P0A7N9(1)|P0A7K6(1)|P68919(1)|P0ADY3(1)|P60438(1)|P60624(1)|P0ADY7(1)|P0ADZ0(1)|P0A7M9(1)|P0A7L3(1)|P0A7L8(1)|P0A7J7(1)|P0A7L0(1)|P0A7J3(1)|P61175(1)|P60422(1)|P60723(1)|P0AG55(1)|P0A7K2(4)|P62399(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit (CPX-3802) which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 30S subunit is responsible for the catalytic activity of the ribosome, the peptidyltransferase activity required to catalyze peptide bond formation. rplL forms dimers with an elongated shape. Two dimers associate with a copy of rplJ to form part of the L8 ribosomal stalk. The ribosomal stalk helps the ribosome interact with GTP-bound translation factors. Hetero39-mer P0A7K2 CPX-3807 50S large ribosomal subunit 50S subunit P0A7P5(1)|P0A7N1(1)|URS000002D309_83333(1)|URS00005B2216_83333(1)|P0A7Q6(1)|P02413(1)|P0A7Q1(1)|P0AG48(1)|P0AG51(1)|P0AG44(1)|P0AA10(1)|P0A7R1(1)|P0A7M2(1)|P0C018(1)|P0A7N4(1)|P0A7M6(1)|P0A7N9(1)|P0A7K6(1)|P68919(1)|P0ADY3(1)|P60438(1)|P60624(1)|P0ADY7(1)|P0ADZ0(1)|P0A7M9(1)|P0A7L3(1)|P0A7L8(1)|P0A7J7(1)|P0A7L0(1)|P0A7J3(1)|P61175(1)|P60422(1)|P60723(1)|P0AG55(1)|P0A7K2(4)|P62399(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit (CPX-3802) which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 30S subunit is responsible for the catalytic activity of the ribosome, the peptidyltransferase activity required to catalyze peptide bond formation. rplL forms dimers with an elongated shape. Two dimers associate with a copy of rplJ to form part of the L8 ribosomal stalk. The ribosomal stalk helps the ribosome interact with GTP-bound translation factors. Hetero39-mer P0A7K6 CPX-3807 50S large ribosomal subunit 50S subunit P0A7P5(1)|P0A7N1(1)|URS000002D309_83333(1)|URS00005B2216_83333(1)|P0A7Q6(1)|P02413(1)|P0A7Q1(1)|P0AG48(1)|P0AG51(1)|P0AG44(1)|P0AA10(1)|P0A7R1(1)|P0A7M2(1)|P0C018(1)|P0A7N4(1)|P0A7M6(1)|P0A7N9(1)|P0A7K6(1)|P68919(1)|P0ADY3(1)|P60438(1)|P60624(1)|P0ADY7(1)|P0ADZ0(1)|P0A7M9(1)|P0A7L3(1)|P0A7L8(1)|P0A7J7(1)|P0A7L0(1)|P0A7J3(1)|P61175(1)|P60422(1)|P60723(1)|P0AG55(1)|P0A7K2(4)|P62399(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit (CPX-3802) which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 30S subunit is responsible for the catalytic activity of the ribosome, the peptidyltransferase activity required to catalyze peptide bond formation. rplL forms dimers with an elongated shape. Two dimers associate with a copy of rplJ to form part of the L8 ribosomal stalk. The ribosomal stalk helps the ribosome interact with GTP-bound translation factors. Hetero39-mer P0A7L0 CPX-3807 50S large ribosomal subunit 50S subunit P0A7P5(1)|P0A7N1(1)|URS000002D309_83333(1)|URS00005B2216_83333(1)|P0A7Q6(1)|P02413(1)|P0A7Q1(1)|P0AG48(1)|P0AG51(1)|P0AG44(1)|P0AA10(1)|P0A7R1(1)|P0A7M2(1)|P0C018(1)|P0A7N4(1)|P0A7M6(1)|P0A7N9(1)|P0A7K6(1)|P68919(1)|P0ADY3(1)|P60438(1)|P60624(1)|P0ADY7(1)|P0ADZ0(1)|P0A7M9(1)|P0A7L3(1)|P0A7L8(1)|P0A7J7(1)|P0A7L0(1)|P0A7J3(1)|P61175(1)|P60422(1)|P60723(1)|P0AG55(1)|P0A7K2(4)|P62399(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit (CPX-3802) which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 30S subunit is responsible for the catalytic activity of the ribosome, the peptidyltransferase activity required to catalyze peptide bond formation. rplL forms dimers with an elongated shape. Two dimers associate with a copy of rplJ to form part of the L8 ribosomal stalk. The ribosomal stalk helps the ribosome interact with GTP-bound translation factors. Hetero39-mer P0A7L8 CPX-3807 50S large ribosomal subunit 50S subunit P0A7P5(1)|P0A7N1(1)|URS000002D309_83333(1)|URS00005B2216_83333(1)|P0A7Q6(1)|P02413(1)|P0A7Q1(1)|P0AG48(1)|P0AG51(1)|P0AG44(1)|P0AA10(1)|P0A7R1(1)|P0A7M2(1)|P0C018(1)|P0A7N4(1)|P0A7M6(1)|P0A7N9(1)|P0A7K6(1)|P68919(1)|P0ADY3(1)|P60438(1)|P60624(1)|P0ADY7(1)|P0ADZ0(1)|P0A7M9(1)|P0A7L3(1)|P0A7L8(1)|P0A7J7(1)|P0A7L0(1)|P0A7J3(1)|P61175(1)|P60422(1)|P60723(1)|P0AG55(1)|P0A7K2(4)|P62399(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit (CPX-3802) which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 30S subunit is responsible for the catalytic activity of the ribosome, the peptidyltransferase activity required to catalyze peptide bond formation. rplL forms dimers with an elongated shape. Two dimers associate with a copy of rplJ to form part of the L8 ribosomal stalk. The ribosomal stalk helps the ribosome interact with GTP-bound translation factors. Hetero39-mer P0A7M2 CPX-3807 50S large ribosomal subunit 50S subunit P0A7P5(1)|P0A7N1(1)|URS000002D309_83333(1)|URS00005B2216_83333(1)|P0A7Q6(1)|P02413(1)|P0A7Q1(1)|P0AG48(1)|P0AG51(1)|P0AG44(1)|P0AA10(1)|P0A7R1(1)|P0A7M2(1)|P0C018(1)|P0A7N4(1)|P0A7M6(1)|P0A7N9(1)|P0A7K6(1)|P68919(1)|P0ADY3(1)|P60438(1)|P60624(1)|P0ADY7(1)|P0ADZ0(1)|P0A7M9(1)|P0A7L3(1)|P0A7L8(1)|P0A7J7(1)|P0A7L0(1)|P0A7J3(1)|P61175(1)|P60422(1)|P60723(1)|P0AG55(1)|P0A7K2(4)|P62399(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit (CPX-3802) which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 30S subunit is responsible for the catalytic activity of the ribosome, the peptidyltransferase activity required to catalyze peptide bond formation. rplL forms dimers with an elongated shape. Two dimers associate with a copy of rplJ to form part of the L8 ribosomal stalk. The ribosomal stalk helps the ribosome interact with GTP-bound translation factors. Hetero39-mer P0A7M6 CPX-3807 50S large ribosomal subunit 50S subunit P0A7P5(1)|P0A7N1(1)|URS000002D309_83333(1)|URS00005B2216_83333(1)|P0A7Q6(1)|P02413(1)|P0A7Q1(1)|P0AG48(1)|P0AG51(1)|P0AG44(1)|P0AA10(1)|P0A7R1(1)|P0A7M2(1)|P0C018(1)|P0A7N4(1)|P0A7M6(1)|P0A7N9(1)|P0A7K6(1)|P68919(1)|P0ADY3(1)|P60438(1)|P60624(1)|P0ADY7(1)|P0ADZ0(1)|P0A7M9(1)|P0A7L3(1)|P0A7L8(1)|P0A7J7(1)|P0A7L0(1)|P0A7J3(1)|P61175(1)|P60422(1)|P60723(1)|P0AG55(1)|P0A7K2(4)|P62399(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit (CPX-3802) which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 30S subunit is responsible for the catalytic activity of the ribosome, the peptidyltransferase activity required to catalyze peptide bond formation. rplL forms dimers with an elongated shape. Two dimers associate with a copy of rplJ to form part of the L8 ribosomal stalk. The ribosomal stalk helps the ribosome interact with GTP-bound translation factors. Hetero39-mer P0A7M9 CPX-3807 50S large ribosomal subunit 50S subunit P0A7P5(1)|P0A7N1(1)|URS000002D309_83333(1)|URS00005B2216_83333(1)|P0A7Q6(1)|P02413(1)|P0A7Q1(1)|P0AG48(1)|P0AG51(1)|P0AG44(1)|P0AA10(1)|P0A7R1(1)|P0A7M2(1)|P0C018(1)|P0A7N4(1)|P0A7M6(1)|P0A7N9(1)|P0A7K6(1)|P68919(1)|P0ADY3(1)|P60438(1)|P60624(1)|P0ADY7(1)|P0ADZ0(1)|P0A7M9(1)|P0A7L3(1)|P0A7L8(1)|P0A7J7(1)|P0A7L0(1)|P0A7J3(1)|P61175(1)|P60422(1)|P60723(1)|P0AG55(1)|P0A7K2(4)|P62399(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit (CPX-3802) which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 30S subunit is responsible for the catalytic activity of the ribosome, the peptidyltransferase activity required to catalyze peptide bond formation. rplL forms dimers with an elongated shape. Two dimers associate with a copy of rplJ to form part of the L8 ribosomal stalk. The ribosomal stalk helps the ribosome interact with GTP-bound translation factors. Hetero39-mer P0A7N1 CPX-3807 50S large ribosomal subunit 50S subunit P0A7P5(1)|P0A7N1(1)|URS000002D309_83333(1)|URS00005B2216_83333(1)|P0A7Q6(1)|P02413(1)|P0A7Q1(1)|P0AG48(1)|P0AG51(1)|P0AG44(1)|P0AA10(1)|P0A7R1(1)|P0A7M2(1)|P0C018(1)|P0A7N4(1)|P0A7M6(1)|P0A7N9(1)|P0A7K6(1)|P68919(1)|P0ADY3(1)|P60438(1)|P60624(1)|P0ADY7(1)|P0ADZ0(1)|P0A7M9(1)|P0A7L3(1)|P0A7L8(1)|P0A7J7(1)|P0A7L0(1)|P0A7J3(1)|P61175(1)|P60422(1)|P60723(1)|P0AG55(1)|P0A7K2(4)|P62399(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit (CPX-3802) which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 30S subunit is responsible for the catalytic activity of the ribosome, the peptidyltransferase activity required to catalyze peptide bond formation. rplL forms dimers with an elongated shape. Two dimers associate with a copy of rplJ to form part of the L8 ribosomal stalk. The ribosomal stalk helps the ribosome interact with GTP-bound translation factors. Hetero39-mer P0A7N4 CPX-3807 50S large ribosomal subunit 50S subunit P0A7P5(1)|P0A7N1(1)|URS000002D309_83333(1)|URS00005B2216_83333(1)|P0A7Q6(1)|P02413(1)|P0A7Q1(1)|P0AG48(1)|P0AG51(1)|P0AG44(1)|P0AA10(1)|P0A7R1(1)|P0A7M2(1)|P0C018(1)|P0A7N4(1)|P0A7M6(1)|P0A7N9(1)|P0A7K6(1)|P68919(1)|P0ADY3(1)|P60438(1)|P60624(1)|P0ADY7(1)|P0ADZ0(1)|P0A7M9(1)|P0A7L3(1)|P0A7L8(1)|P0A7J7(1)|P0A7L0(1)|P0A7J3(1)|P61175(1)|P60422(1)|P60723(1)|P0AG55(1)|P0A7K2(4)|P62399(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit (CPX-3802) which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 30S subunit is responsible for the catalytic activity of the ribosome, the peptidyltransferase activity required to catalyze peptide bond formation. rplL forms dimers with an elongated shape. Two dimers associate with a copy of rplJ to form part of the L8 ribosomal stalk. The ribosomal stalk helps the ribosome interact with GTP-bound translation factors. Hetero39-mer P0A7R1 CPX-3807 50S large ribosomal subunit 50S subunit P0A7P5(1)|P0A7N1(1)|URS000002D309_83333(1)|URS00005B2216_83333(1)|P0A7Q6(1)|P02413(1)|P0A7Q1(1)|P0AG48(1)|P0AG51(1)|P0AG44(1)|P0AA10(1)|P0A7R1(1)|P0A7M2(1)|P0C018(1)|P0A7N4(1)|P0A7M6(1)|P0A7N9(1)|P0A7K6(1)|P68919(1)|P0ADY3(1)|P60438(1)|P60624(1)|P0ADY7(1)|P0ADZ0(1)|P0A7M9(1)|P0A7L3(1)|P0A7L8(1)|P0A7J7(1)|P0A7L0(1)|P0A7J3(1)|P61175(1)|P60422(1)|P60723(1)|P0AG55(1)|P0A7K2(4)|P62399(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit (CPX-3802) which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 30S subunit is responsible for the catalytic activity of the ribosome, the peptidyltransferase activity required to catalyze peptide bond formation. rplL forms dimers with an elongated shape. Two dimers associate with a copy of rplJ to form part of the L8 ribosomal stalk. The ribosomal stalk helps the ribosome interact with GTP-bound translation factors. Hetero39-mer P0A7R9 CPX-3802 30S small ribosomal subunit 30S subunit P68679(1)|URS00005CADE5_83333(1)|P0A7R5(1)|P0A7X3(1)|P0A7T3(1)|P0A7U3(1)|P0A7U7(1)|P0A7V3(1)|P0A7R9(1)|P0A7W7(1)|P0A7T7(1)|P0AG63(1)|P0A7V0(1)|P0ADZ4(1)|P0A7S3(1)|P0A7V8(1)|P0A7W1(1)|P0A7S9(1)|P02359(1)|P0AG67(1)|P02358(1)|P0AG59(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit (CPX-3807) which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 50S subunit acts as the decoding centre of the ribosome which brings mRNA and aminoacylated transfer (t)RNAs together, with the 16S ribosomal (r)RNA being required for the selection of the cognate tRNA. Guides the initiating start codon AUG of mRNA into position by recognizing the Shine-Dalgarno sequence, a complementary binding site about 8 base pairs upstream from the start codon. In order to form the translation complex with the 50S subunit, the 30S subunit must bind the Translation Initiation factor complex (CPX-2244), mRNA, and f-met-tRNA. The mRNA entrance channel is formed mainly by proteins rpsC, rpsD, and rpsE. Hetero22-mer P0A7S3 CPX-3802 30S small ribosomal subunit 30S subunit P68679(1)|URS00005CADE5_83333(1)|P0A7R5(1)|P0A7X3(1)|P0A7T3(1)|P0A7U3(1)|P0A7U7(1)|P0A7V3(1)|P0A7R9(1)|P0A7W7(1)|P0A7T7(1)|P0AG63(1)|P0A7V0(1)|P0ADZ4(1)|P0A7S3(1)|P0A7V8(1)|P0A7W1(1)|P0A7S9(1)|P02359(1)|P0AG67(1)|P02358(1)|P0AG59(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit (CPX-3807) which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 50S subunit acts as the decoding centre of the ribosome which brings mRNA and aminoacylated transfer (t)RNAs together, with the 16S ribosomal (r)RNA being required for the selection of the cognate tRNA. Guides the initiating start codon AUG of mRNA into position by recognizing the Shine-Dalgarno sequence, a complementary binding site about 8 base pairs upstream from the start codon. In order to form the translation complex with the 50S subunit, the 30S subunit must bind the Translation Initiation factor complex (CPX-2244), mRNA, and f-met-tRNA. The mRNA entrance channel is formed mainly by proteins rpsC, rpsD, and rpsE. Hetero22-mer P0A7S9 CPX-3802 30S small ribosomal subunit 30S subunit P68679(1)|URS00005CADE5_83333(1)|P0A7R5(1)|P0A7X3(1)|P0A7T3(1)|P0A7U3(1)|P0A7U7(1)|P0A7V3(1)|P0A7R9(1)|P0A7W7(1)|P0A7T7(1)|P0AG63(1)|P0A7V0(1)|P0ADZ4(1)|P0A7S3(1)|P0A7V8(1)|P0A7W1(1)|P0A7S9(1)|P02359(1)|P0AG67(1)|P02358(1)|P0AG59(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit (CPX-3807) which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 50S subunit acts as the decoding centre of the ribosome which brings mRNA and aminoacylated transfer (t)RNAs together, with the 16S ribosomal (r)RNA being required for the selection of the cognate tRNA. Guides the initiating start codon AUG of mRNA into position by recognizing the Shine-Dalgarno sequence, a complementary binding site about 8 base pairs upstream from the start codon. In order to form the translation complex with the 50S subunit, the 30S subunit must bind the Translation Initiation factor complex (CPX-2244), mRNA, and f-met-tRNA. The mRNA entrance channel is formed mainly by proteins rpsC, rpsD, and rpsE. Hetero22-mer P0A7T3 CPX-3802 30S small ribosomal subunit 30S subunit P68679(1)|URS00005CADE5_83333(1)|P0A7R5(1)|P0A7X3(1)|P0A7T3(1)|P0A7U3(1)|P0A7U7(1)|P0A7V3(1)|P0A7R9(1)|P0A7W7(1)|P0A7T7(1)|P0AG63(1)|P0A7V0(1)|P0ADZ4(1)|P0A7S3(1)|P0A7V8(1)|P0A7W1(1)|P0A7S9(1)|P02359(1)|P0AG67(1)|P02358(1)|P0AG59(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit (CPX-3807) which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 50S subunit acts as the decoding centre of the ribosome which brings mRNA and aminoacylated transfer (t)RNAs together, with the 16S ribosomal (r)RNA being required for the selection of the cognate tRNA. Guides the initiating start codon AUG of mRNA into position by recognizing the Shine-Dalgarno sequence, a complementary binding site about 8 base pairs upstream from the start codon. In order to form the translation complex with the 50S subunit, the 30S subunit must bind the Translation Initiation factor complex (CPX-2244), mRNA, and f-met-tRNA. The mRNA entrance channel is formed mainly by proteins rpsC, rpsD, and rpsE. Hetero22-mer P0A7T7 CPX-3802 30S small ribosomal subunit 30S subunit P68679(1)|URS00005CADE5_83333(1)|P0A7R5(1)|P0A7X3(1)|P0A7T3(1)|P0A7U3(1)|P0A7U7(1)|P0A7V3(1)|P0A7R9(1)|P0A7W7(1)|P0A7T7(1)|P0AG63(1)|P0A7V0(1)|P0ADZ4(1)|P0A7S3(1)|P0A7V8(1)|P0A7W1(1)|P0A7S9(1)|P02359(1)|P0AG67(1)|P02358(1)|P0AG59(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit (CPX-3807) which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 50S subunit acts as the decoding centre of the ribosome which brings mRNA and aminoacylated transfer (t)RNAs together, with the 16S ribosomal (r)RNA being required for the selection of the cognate tRNA. Guides the initiating start codon AUG of mRNA into position by recognizing the Shine-Dalgarno sequence, a complementary binding site about 8 base pairs upstream from the start codon. In order to form the translation complex with the 50S subunit, the 30S subunit must bind the Translation Initiation factor complex (CPX-2244), mRNA, and f-met-tRNA. The mRNA entrance channel is formed mainly by proteins rpsC, rpsD, and rpsE. Hetero22-mer P0A7U3 CPX-3802 30S small ribosomal subunit 30S subunit P68679(1)|URS00005CADE5_83333(1)|P0A7R5(1)|P0A7X3(1)|P0A7T3(1)|P0A7U3(1)|P0A7U7(1)|P0A7V3(1)|P0A7R9(1)|P0A7W7(1)|P0A7T7(1)|P0AG63(1)|P0A7V0(1)|P0ADZ4(1)|P0A7S3(1)|P0A7V8(1)|P0A7W1(1)|P0A7S9(1)|P02359(1)|P0AG67(1)|P02358(1)|P0AG59(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit (CPX-3807) which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 50S subunit acts as the decoding centre of the ribosome which brings mRNA and aminoacylated transfer (t)RNAs together, with the 16S ribosomal (r)RNA being required for the selection of the cognate tRNA. Guides the initiating start codon AUG of mRNA into position by recognizing the Shine-Dalgarno sequence, a complementary binding site about 8 base pairs upstream from the start codon. In order to form the translation complex with the 50S subunit, the 30S subunit must bind the Translation Initiation factor complex (CPX-2244), mRNA, and f-met-tRNA. The mRNA entrance channel is formed mainly by proteins rpsC, rpsD, and rpsE. Hetero22-mer P0A7V0 CPX-3802 30S small ribosomal subunit 30S subunit P68679(1)|URS00005CADE5_83333(1)|P0A7R5(1)|P0A7X3(1)|P0A7T3(1)|P0A7U3(1)|P0A7U7(1)|P0A7V3(1)|P0A7R9(1)|P0A7W7(1)|P0A7T7(1)|P0AG63(1)|P0A7V0(1)|P0ADZ4(1)|P0A7S3(1)|P0A7V8(1)|P0A7W1(1)|P0A7S9(1)|P02359(1)|P0AG67(1)|P02358(1)|P0AG59(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit (CPX-3807) which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 50S subunit acts as the decoding centre of the ribosome which brings mRNA and aminoacylated transfer (t)RNAs together, with the 16S ribosomal (r)RNA being required for the selection of the cognate tRNA. Guides the initiating start codon AUG of mRNA into position by recognizing the Shine-Dalgarno sequence, a complementary binding site about 8 base pairs upstream from the start codon. In order to form the translation complex with the 50S subunit, the 30S subunit must bind the Translation Initiation factor complex (CPX-2244), mRNA, and f-met-tRNA. The mRNA entrance channel is formed mainly by proteins rpsC, rpsD, and rpsE. Hetero22-mer P0A7V3 CPX-3802 30S small ribosomal subunit 30S subunit P68679(1)|URS00005CADE5_83333(1)|P0A7R5(1)|P0A7X3(1)|P0A7T3(1)|P0A7U3(1)|P0A7U7(1)|P0A7V3(1)|P0A7R9(1)|P0A7W7(1)|P0A7T7(1)|P0AG63(1)|P0A7V0(1)|P0ADZ4(1)|P0A7S3(1)|P0A7V8(1)|P0A7W1(1)|P0A7S9(1)|P02359(1)|P0AG67(1)|P02358(1)|P0AG59(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit (CPX-3807) which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 50S subunit acts as the decoding centre of the ribosome which brings mRNA and aminoacylated transfer (t)RNAs together, with the 16S ribosomal (r)RNA being required for the selection of the cognate tRNA. Guides the initiating start codon AUG of mRNA into position by recognizing the Shine-Dalgarno sequence, a complementary binding site about 8 base pairs upstream from the start codon. In order to form the translation complex with the 50S subunit, the 30S subunit must bind the Translation Initiation factor complex (CPX-2244), mRNA, and f-met-tRNA. The mRNA entrance channel is formed mainly by proteins rpsC, rpsD, and rpsE. Hetero22-mer P0A7V8 CPX-3802 30S small ribosomal subunit 30S subunit P68679(1)|URS00005CADE5_83333(1)|P0A7R5(1)|P0A7X3(1)|P0A7T3(1)|P0A7U3(1)|P0A7U7(1)|P0A7V3(1)|P0A7R9(1)|P0A7W7(1)|P0A7T7(1)|P0AG63(1)|P0A7V0(1)|P0ADZ4(1)|P0A7S3(1)|P0A7V8(1)|P0A7W1(1)|P0A7S9(1)|P02359(1)|P0AG67(1)|P02358(1)|P0AG59(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit (CPX-3807) which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 50S subunit acts as the decoding centre of the ribosome which brings mRNA and aminoacylated transfer (t)RNAs together, with the 16S ribosomal (r)RNA being required for the selection of the cognate tRNA. Guides the initiating start codon AUG of mRNA into position by recognizing the Shine-Dalgarno sequence, a complementary binding site about 8 base pairs upstream from the start codon. In order to form the translation complex with the 50S subunit, the 30S subunit must bind the Translation Initiation factor complex (CPX-2244), mRNA, and f-met-tRNA. The mRNA entrance channel is formed mainly by proteins rpsC, rpsD, and rpsE. Hetero22-mer P0A7W1 CPX-3802 30S small ribosomal subunit 30S subunit P68679(1)|URS00005CADE5_83333(1)|P0A7R5(1)|P0A7X3(1)|P0A7T3(1)|P0A7U3(1)|P0A7U7(1)|P0A7V3(1)|P0A7R9(1)|P0A7W7(1)|P0A7T7(1)|P0AG63(1)|P0A7V0(1)|P0ADZ4(1)|P0A7S3(1)|P0A7V8(1)|P0A7W1(1)|P0A7S9(1)|P02359(1)|P0AG67(1)|P02358(1)|P0AG59(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit (CPX-3807) which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 50S subunit acts as the decoding centre of the ribosome which brings mRNA and aminoacylated transfer (t)RNAs together, with the 16S ribosomal (r)RNA being required for the selection of the cognate tRNA. Guides the initiating start codon AUG of mRNA into position by recognizing the Shine-Dalgarno sequence, a complementary binding site about 8 base pairs upstream from the start codon. In order to form the translation complex with the 50S subunit, the 30S subunit must bind the Translation Initiation factor complex (CPX-2244), mRNA, and f-met-tRNA. The mRNA entrance channel is formed mainly by proteins rpsC, rpsD, and rpsE. Hetero22-mer P0A7W7 CPX-3802 30S small ribosomal subunit 30S subunit P68679(1)|URS00005CADE5_83333(1)|P0A7R5(1)|P0A7X3(1)|P0A7T3(1)|P0A7U3(1)|P0A7U7(1)|P0A7V3(1)|P0A7R9(1)|P0A7W7(1)|P0A7T7(1)|P0AG63(1)|P0A7V0(1)|P0ADZ4(1)|P0A7S3(1)|P0A7V8(1)|P0A7W1(1)|P0A7S9(1)|P02359(1)|P0AG67(1)|P02358(1)|P0AG59(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit (CPX-3807) which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 50S subunit acts as the decoding centre of the ribosome which brings mRNA and aminoacylated transfer (t)RNAs together, with the 16S ribosomal (r)RNA being required for the selection of the cognate tRNA. Guides the initiating start codon AUG of mRNA into position by recognizing the Shine-Dalgarno sequence, a complementary binding site about 8 base pairs upstream from the start codon. In order to form the translation complex with the 50S subunit, the 30S subunit must bind the Translation Initiation factor complex (CPX-2244), mRNA, and f-met-tRNA. The mRNA entrance channel is formed mainly by proteins rpsC, rpsD, and rpsE. Hetero22-mer P0A7X3 CPX-3802 30S small ribosomal subunit 30S subunit P68679(1)|URS00005CADE5_83333(1)|P0A7R5(1)|P0A7X3(1)|P0A7T3(1)|P0A7U3(1)|P0A7U7(1)|P0A7V3(1)|P0A7R9(1)|P0A7W7(1)|P0A7T7(1)|P0AG63(1)|P0A7V0(1)|P0ADZ4(1)|P0A7S3(1)|P0A7V8(1)|P0A7W1(1)|P0A7S9(1)|P02359(1)|P0AG67(1)|P02358(1)|P0AG59(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit (CPX-3807) which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 50S subunit acts as the decoding centre of the ribosome which brings mRNA and aminoacylated transfer (t)RNAs together, with the 16S ribosomal (r)RNA being required for the selection of the cognate tRNA. Guides the initiating start codon AUG of mRNA into position by recognizing the Shine-Dalgarno sequence, a complementary binding site about 8 base pairs upstream from the start codon. In order to form the translation complex with the 50S subunit, the 30S subunit must bind the Translation Initiation factor complex (CPX-2244), mRNA, and f-met-tRNA. The mRNA entrance channel is formed mainly by proteins rpsC, rpsD, and rpsE. Hetero22-mer P0A836 CPX-1092 Succinyl-CoA synthetase - P0A836(2)|P0AGE9(2)|CHEBI:18420(2) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-1770945 Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. It catalyzes the reversible interchange of purine nucleoside diphosphate, succinyl-CoA and phosphate with purine nucleoside triphosphate, succinate, and CoA via a phosphorylated histidine intermediate. The alpha subunit (sucC) of the enzyme binds the substrates CoA and phosphate. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate. During catalysis the histidine residue of alpha subunit (His-246) is transiently phosphorylated. Heterotetramer P0A877 CPX-3446 TrpAB tryptophan synthase complex trpAB complex|TrpA-TrpB tryptophan synthase complex CHEBI:597326(1)|P0A879(2)|P0A877(2) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Catalyzes the final two steps in the biosynthesis of L-tryptophan. Complex formation stimulates the separate enzymatic activities of the alpha and beta subunit by one to two orders of magnitude, due to conformational changes of the subunits on binding. The alpha-subunit catalyses the cleavage of indole-glycerol-phosphate to indole and glyceraldehyde-3-phosphate. In the beta-subunit, indole is condensed with l-serine to l-tryptophan and water in a pyridoxal-5-prime-phosphate dependent reaction. Indole diffuses from the alpha to the beta-active site through a tunnel formed by the subunits, preventing its loss through absorption by the cell membranes The alpha- and beta-subunits are arranged in a linear alpha-beta-beta=alpha fashion with the active centers of each alpha and beta-dimeric unit interconnected by a 25A long tunnel. Heterotetramer P0A9H9 CPX-1088 Chemotaxis phosphorelay complex CheY-CheZ - CHEBI:18420(1)|CHEBI:18420(1)|P0A9H9(1)|P0AE67(1)|P0AE67(1)|P0A9H9(1) ECO:0000353(physical interaction evidence used in manual assertion) - Plays a role in chemotaxis, the movement toward or away from chemicals. The flagellar motor of bacteria is a rotary device energized by the membrane ion gradient and the complex is required for the rotation and directional switching of the flagellum and also functions in flagellar assembly. Motor torque is produced at the top of the switch complex, where the fliG C-terminal domain bears several conserved charged residues that interact with charged groups of the stator protein motA (P09348). The directionality of the rotation is determined by binding of cheY-P to the lower part of the C-ring which switches the directionality from counter-clockwise to clockwise. The cheY-cheZ complex enhances the dephosphorylation rate of P-cheY. This dephosphorylation reduces the binding of cheY to the switch and ensures rapid locomotor responses to changes in the supply of signaling phosphoryl groups to cheY, thus enabling a continuous response to environmental changes. The side chain of Gln-147 of cheZ inserts into the cheY active site, filling one coordination site of the Mg2+, and rendering the existing mechanism of CheY autodephosphorylation more efficient by positioning a water molecule in the appropriate geometry for nucleophilic attack. Heterotetramer P0A9H9 CPX-1088 Chemotaxis phosphorelay complex CheY-CheZ - CHEBI:18420(1)|CHEBI:18420(1)|P0A9H9(1)|P0AE67(1)|P0AE67(1)|P0A9H9(1) ECO:0000353(physical interaction evidence used in manual assertion) - Plays a role in chemotaxis, the movement toward or away from chemicals. The flagellar motor of bacteria is a rotary device energized by the membrane ion gradient and the complex is required for the rotation and directional switching of the flagellum and also functions in flagellar assembly. Motor torque is produced at the top of the switch complex, where the fliG C-terminal domain bears several conserved charged residues that interact with charged groups of the stator protein motA (P09348). The directionality of the rotation is determined by binding of cheY-P to the lower part of the C-ring which switches the directionality from counter-clockwise to clockwise. The cheY-cheZ complex enhances the dephosphorylation rate of P-cheY. This dephosphorylation reduces the binding of cheY to the switch and ensures rapid locomotor responses to changes in the supply of signaling phosphoryl groups to cheY, thus enabling a continuous response to environmental changes. The side chain of Gln-147 of cheZ inserts into the cheY active site, filling one coordination site of the Mg2+, and rendering the existing mechanism of CheY autodephosphorylation more efficient by positioning a water molecule in the appropriate geometry for nucleophilic attack. Heterotetramer P0A9P0 CPX-3943 Pyruvate dehydrogenase complex PDH complex|dihydrolipoyl dehydrogenase complex|PDHC P0A9P0(12)|P0AFG8(24)|P06959(24)|CHEBI:57692(12)|CHEBI:83088(0)|CHEBI:58937(0)|CHEBI:18420(0) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Converts pyruvate to acetyl-CoA and CO2, thus providing a metabolic connection between glycolysis, whose end product is pyruvate, and the tricarboxylic acid cycle, which starts with acetyl-CoA. It contains multiple copies of three enzymatic components, that are encoded by a single operon: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). In anaerobic Escherichia coli, the complex is normally inactive due to inhibition of ldpA by NADH. During aerobic growth, the NADH generated in glycolysis is oxidized and the complex becomes active. Assembled symmetrically around a 24-polypeptide structural core with octahedral symmetry built mainly from catalytic domains in the aceF components, with the peripheral aceE and lpdA components displaced and separated from the core by large distances but tethered to it by flexible linkers non-covalently bound to them. - P0A9P0 CPX-3921 2-oxoglutarate dehydrogenase complex alpha-Ketoglutarate dehydrogenase complex|OGDH complex|dihydrolipoamide S-succinyltransferase complex P0A9P0(1)|CHEBI:57692(1)|CHEBI:58937(0)|CHEBI:83088(0)|P0AFG3(12)|P0AFG6(24)|P0A9P0(1)|CHEBI:57692(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Multi-enzyme complex that catalyzes the conversion of 2-oxoglutarate (2-ketoglutarate) to succinyl-CoA and CO2, with the production of NADH, during the citric acid cycle. It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3). 2-oxoglutarate is bound and decarboxylated by sucA, sucB catalyzes the transfer of a succinyl group from the S-succinyldihydrolipoyl moiety to coenzyme A, forming succinyl-CoA and lpdA catalyzes the transfer of electrons to the ultimate acceptor, NAD. sucA and lpdA are recruited through direct interaction with sucB, which is an oligomeric enzyme with structurally distinct domains that are linked by flexible regions of polypeptide chain of 28â€?0 residues that are rich in Ala and Pro. Hetero28-mer P0A9P0 CPX-3921 2-oxoglutarate dehydrogenase complex alpha-Ketoglutarate dehydrogenase complex|OGDH complex|dihydrolipoamide S-succinyltransferase complex P0A9P0(1)|CHEBI:57692(1)|CHEBI:58937(0)|CHEBI:83088(0)|P0AFG3(12)|P0AFG6(24)|P0A9P0(1)|CHEBI:57692(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Multi-enzyme complex that catalyzes the conversion of 2-oxoglutarate (2-ketoglutarate) to succinyl-CoA and CO2, with the production of NADH, during the citric acid cycle. It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3). 2-oxoglutarate is bound and decarboxylated by sucA, sucB catalyzes the transfer of a succinyl group from the S-succinyldihydrolipoyl moiety to coenzyme A, forming succinyl-CoA and lpdA catalyzes the transfer of electrons to the ultimate acceptor, NAD. sucA and lpdA are recruited through direct interaction with sucB, which is an oligomeric enzyme with structurally distinct domains that are linked by flexible regions of polypeptide chain of 28â€?0 residues that are rich in Ala and Pro. Hetero28-mer P0A9P0 CPX-3949 Glycine cleavage system complex Gycine decarboxylase complex|Glycine cleavage complex|gcvP/T/L/H complex P0A9P0(0)|P27248(0)|P0A6T9(0)|P33195(0)|CHEBI:597326(0)|CHEBI:57692(0)|CHEBI:83088(0) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Multienzyme complex that catalyses the reversible oxidation of glycine, yielding carbon dioxide (CO), ammonia (NH3), 5,10-methylenetetrahydrofolate and a reduced pyridine nucleotide. The 1-carbon units thus generated are used in the synthesis of purines, histidine, thymine, pantothenate, and methionine and in the formylation of the aminoacylated initiator fMet-TRNAfMet required for translation initiation. gcvP binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO2 is released and the remaining methylamine moiety is transferred to the lipoamide cofactor of gcvH, which is bound to the P protein prior to decarboxylation of glycine. gcvT catalyzes the release of NH3 from the methylamine group and transfers the remaining C1 unit to tetrahydrofolate, forming 5,10-methylenetetrahydrofolate. lpdA then oxidizes the lipoic acid component of the H protein and transfers the electrons to NAD+, to form NADH . - - P0AA10 CPX-3807 50S large ribosomal subunit 50S subunit P0A7P5(1)|P0A7N1(1)|URS000002D309_83333(1)|URS00005B2216_83333(1)|P0A7Q6(1)|P02413(1)|P0A7Q1(1)|P0AG48(1)|P0AG51(1)|P0AG44(1)|P0AA10(1)|P0A7R1(1)|P0A7M2(1)|P0C018(1)|P0A7N4(1)|P0A7M6(1)|P0A7N9(1)|P0A7K6(1)|P68919(1)|P0ADY3(1)|P60438(1)|P60624(1)|P0ADY7(1)|P0ADZ0(1)|P0A7M9(1)|P0A7L3(1)|P0A7L8(1)|P0A7J7(1)|P0A7L0(1)|P0A7J3(1)|P61175(1)|P60422(1)|P60723(1)|P0AG55(1)|P0A7K2(4)|P62399(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit (CPX-3802) which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 30S subunit is responsible for the catalytic activity of the ribosome, the peptidyltransferase activity required to catalyze peptide bond formation. rplL forms dimers with an elongated shape. Two dimers associate with a copy of rplJ to form part of the L8 ribosomal stalk. The ribosomal stalk helps the ribosome interact with GTP-bound translation factors. Hetero39-mer P0AB18 CPX-2145 TusE-MnmA complex - P0AB18(1)|P25745(1)|CHEBI:17843(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-8871587 Involved in the sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm5s2U) at tRNA wobble positions. The TusE subunit transfers sulfur (most likely bound to Cys108 as persulfide) from the TusBCDE complex (CPX-2144) to the tRNA. - - P0AB18 CPX-2144 TusBCDE complex TusBCD-TusE complex P45530(2)|P45531(2)|P0AB18(1)|P45532(2) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-8871626 Involved in the sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm5s2U) at tRNA wobble positions. It transfers sulfur (most likely in persulfide form) from TusA (P0A890) to the TusE-MnmA complex (CPX-2145) via Cys78-TusD and Cys108-TusE. Although TusBCD complex has been crystallised it has not yet been shown experimentally that it exists in vivo without subunit TusE attached. Heteroseptamer. - P0ABA0 CPX-4022 ATP synthase complex F-ATPase complex P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P0ABB4(1)|P0ABB0(1)|P0ABB0(1)|P0ABB4(1)|P0ABA4(1)|P0ABA0(2)|P0ABA6(1)|P0A6E6(1)|P0ABB4(1)|P0ABB0(1)|P0AB98(1)|P68699(1) ECO:0000353(physical interaction evidence used in manual assertion) wwpdb:5t4q Acts to convert the energy of oxidation-reduction reactions of the electron transport chain (respiration) to the phosphorylation of ADP. The synthesis of ATP is coupled to the respiratory chain via the proton potential. The ATP synthase is a molecular motor composed of two separable parts: F1 and F0. The F0 motor spans the membrane converting the potential energy of the proton motive force (pmf) into rotation of the central stalk that in turn drives conformational changes in the F1 catalytic sites. Bacterial F-ATPase can also function in reverse, employing ATP hydrolysis to generate a proton gradient across the membrane when needed The F0 motor is constructed from three proteins, atpB, atpE and atpF. atpE assembles into a ring with probable decameric stoichiometry whereas atpB and atpF associate to form a helical bundle adjacent to this ring. The motor comprises a ring of three heterodimers, each containing an active site at the interface of subunits atpA and atpD. Within the F1 motor, each atpA--atpD dimer has a different conformation at any point in time and can be either empty, bound to ADP and phosphate, or bound to ATP (open, half-closed, closed) Hetero 22-mer P0ABB0 CPX-4022 ATP synthase complex F-ATPase complex P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P0ABB4(1)|P0ABB0(1)|P0ABB0(1)|P0ABB4(1)|P0ABA4(1)|P0ABA0(2)|P0ABA6(1)|P0A6E6(1)|P0ABB4(1)|P0ABB0(1)|P0AB98(1)|P68699(1) ECO:0000353(physical interaction evidence used in manual assertion) wwpdb:5t4q Acts to convert the energy of oxidation-reduction reactions of the electron transport chain (respiration) to the phosphorylation of ADP. The synthesis of ATP is coupled to the respiratory chain via the proton potential. The ATP synthase is a molecular motor composed of two separable parts: F1 and F0. The F0 motor spans the membrane converting the potential energy of the proton motive force (pmf) into rotation of the central stalk that in turn drives conformational changes in the F1 catalytic sites. Bacterial F-ATPase can also function in reverse, employing ATP hydrolysis to generate a proton gradient across the membrane when needed The F0 motor is constructed from three proteins, atpB, atpE and atpF. atpE assembles into a ring with probable decameric stoichiometry whereas atpB and atpF associate to form a helical bundle adjacent to this ring. The motor comprises a ring of three heterodimers, each containing an active site at the interface of subunits atpA and atpD. Within the F1 motor, each atpA--atpD dimer has a different conformation at any point in time and can be either empty, bound to ADP and phosphate, or bound to ATP (open, half-closed, closed) Hetero 22-mer P0ABB0 CPX-4022 ATP synthase complex F-ATPase complex P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P0ABB4(1)|P0ABB0(1)|P0ABB0(1)|P0ABB4(1)|P0ABA4(1)|P0ABA0(2)|P0ABA6(1)|P0A6E6(1)|P0ABB4(1)|P0ABB0(1)|P0AB98(1)|P68699(1) ECO:0000353(physical interaction evidence used in manual assertion) wwpdb:5t4q Acts to convert the energy of oxidation-reduction reactions of the electron transport chain (respiration) to the phosphorylation of ADP. The synthesis of ATP is coupled to the respiratory chain via the proton potential. The ATP synthase is a molecular motor composed of two separable parts: F1 and F0. The F0 motor spans the membrane converting the potential energy of the proton motive force (pmf) into rotation of the central stalk that in turn drives conformational changes in the F1 catalytic sites. Bacterial F-ATPase can also function in reverse, employing ATP hydrolysis to generate a proton gradient across the membrane when needed The F0 motor is constructed from three proteins, atpB, atpE and atpF. atpE assembles into a ring with probable decameric stoichiometry whereas atpB and atpF associate to form a helical bundle adjacent to this ring. The motor comprises a ring of three heterodimers, each containing an active site at the interface of subunits atpA and atpD. Within the F1 motor, each atpA--atpD dimer has a different conformation at any point in time and can be either empty, bound to ADP and phosphate, or bound to ATP (open, half-closed, closed) Hetero 22-mer P0ABB0 CPX-4022 ATP synthase complex F-ATPase complex P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P0ABB4(1)|P0ABB0(1)|P0ABB0(1)|P0ABB4(1)|P0ABA4(1)|P0ABA0(2)|P0ABA6(1)|P0A6E6(1)|P0ABB4(1)|P0ABB0(1)|P0AB98(1)|P68699(1) ECO:0000353(physical interaction evidence used in manual assertion) wwpdb:5t4q Acts to convert the energy of oxidation-reduction reactions of the electron transport chain (respiration) to the phosphorylation of ADP. The synthesis of ATP is coupled to the respiratory chain via the proton potential. The ATP synthase is a molecular motor composed of two separable parts: F1 and F0. The F0 motor spans the membrane converting the potential energy of the proton motive force (pmf) into rotation of the central stalk that in turn drives conformational changes in the F1 catalytic sites. Bacterial F-ATPase can also function in reverse, employing ATP hydrolysis to generate a proton gradient across the membrane when needed The F0 motor is constructed from three proteins, atpB, atpE and atpF. atpE assembles into a ring with probable decameric stoichiometry whereas atpB and atpF associate to form a helical bundle adjacent to this ring. The motor comprises a ring of three heterodimers, each containing an active site at the interface of subunits atpA and atpD. Within the F1 motor, each atpA--atpD dimer has a different conformation at any point in time and can be either empty, bound to ADP and phosphate, or bound to ATP (open, half-closed, closed) Hetero 22-mer P0ABB4 CPX-4022 ATP synthase complex F-ATPase complex P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P0ABB4(1)|P0ABB0(1)|P0ABB0(1)|P0ABB4(1)|P0ABA4(1)|P0ABA0(2)|P0ABA6(1)|P0A6E6(1)|P0ABB4(1)|P0ABB0(1)|P0AB98(1)|P68699(1) ECO:0000353(physical interaction evidence used in manual assertion) wwpdb:5t4q Acts to convert the energy of oxidation-reduction reactions of the electron transport chain (respiration) to the phosphorylation of ADP. The synthesis of ATP is coupled to the respiratory chain via the proton potential. The ATP synthase is a molecular motor composed of two separable parts: F1 and F0. The F0 motor spans the membrane converting the potential energy of the proton motive force (pmf) into rotation of the central stalk that in turn drives conformational changes in the F1 catalytic sites. Bacterial F-ATPase can also function in reverse, employing ATP hydrolysis to generate a proton gradient across the membrane when needed The F0 motor is constructed from three proteins, atpB, atpE and atpF. atpE assembles into a ring with probable decameric stoichiometry whereas atpB and atpF associate to form a helical bundle adjacent to this ring. The motor comprises a ring of three heterodimers, each containing an active site at the interface of subunits atpA and atpD. Within the F1 motor, each atpA--atpD dimer has a different conformation at any point in time and can be either empty, bound to ADP and phosphate, or bound to ATP (open, half-closed, closed) Hetero 22-mer P0ABB4 CPX-4022 ATP synthase complex F-ATPase complex P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P0ABB4(1)|P0ABB0(1)|P0ABB0(1)|P0ABB4(1)|P0ABA4(1)|P0ABA0(2)|P0ABA6(1)|P0A6E6(1)|P0ABB4(1)|P0ABB0(1)|P0AB98(1)|P68699(1) ECO:0000353(physical interaction evidence used in manual assertion) wwpdb:5t4q Acts to convert the energy of oxidation-reduction reactions of the electron transport chain (respiration) to the phosphorylation of ADP. The synthesis of ATP is coupled to the respiratory chain via the proton potential. The ATP synthase is a molecular motor composed of two separable parts: F1 and F0. The F0 motor spans the membrane converting the potential energy of the proton motive force (pmf) into rotation of the central stalk that in turn drives conformational changes in the F1 catalytic sites. Bacterial F-ATPase can also function in reverse, employing ATP hydrolysis to generate a proton gradient across the membrane when needed The F0 motor is constructed from three proteins, atpB, atpE and atpF. atpE assembles into a ring with probable decameric stoichiometry whereas atpB and atpF associate to form a helical bundle adjacent to this ring. The motor comprises a ring of three heterodimers, each containing an active site at the interface of subunits atpA and atpD. Within the F1 motor, each atpA--atpD dimer has a different conformation at any point in time and can be either empty, bound to ADP and phosphate, or bound to ATP (open, half-closed, closed) Hetero 22-mer P0ABB4 CPX-4022 ATP synthase complex F-ATPase complex P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P68699(1)|P0ABB4(1)|P0ABB0(1)|P0ABB0(1)|P0ABB4(1)|P0ABA4(1)|P0ABA0(2)|P0ABA6(1)|P0A6E6(1)|P0ABB4(1)|P0ABB0(1)|P0AB98(1)|P68699(1) ECO:0000353(physical interaction evidence used in manual assertion) wwpdb:5t4q Acts to convert the energy of oxidation-reduction reactions of the electron transport chain (respiration) to the phosphorylation of ADP. The synthesis of ATP is coupled to the respiratory chain via the proton potential. The ATP synthase is a molecular motor composed of two separable parts: F1 and F0. The F0 motor spans the membrane converting the potential energy of the proton motive force (pmf) into rotation of the central stalk that in turn drives conformational changes in the F1 catalytic sites. Bacterial F-ATPase can also function in reverse, employing ATP hydrolysis to generate a proton gradient across the membrane when needed The F0 motor is constructed from three proteins, atpB, atpE and atpF. atpE assembles into a ring with probable decameric stoichiometry whereas atpB and atpF associate to form a helical bundle adjacent to this ring. The motor comprises a ring of three heterodimers, each containing an active site at the interface of subunits atpA and atpD. Within the F1 motor, each atpA--atpD dimer has a different conformation at any point in time and can be either empty, bound to ADP and phosphate, or bound to ATP (open, half-closed, closed) Hetero 22-mer P0ABD5 CPX-3206 Acetyl-CoA carboxylase complex ACC complex|Biotin-dependent acetyl-coenzyme A carboxylase complex|ACCase complex CHEBI:15956(1)|P0ABD8(1)|CHEBI:15956(1)|CHEBI:15956(1)|P24182(2)|P0A9Q5(1)|CHEBI:29105(1)|P0ABD8(1)|P0ABD8(1)|CHEBI:29105(1)|P0A9Q5(1)|P0ABD5(2)|CHEBI:15956(1)|P0ABD8(1)|P24182(2) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Biotin-dependent, multifunctional enzyme that catalyzes the first committed step in fatty acid synthesis.The overall reaction is the biotin-dependent carboxylation of acetyl-CoA to form malonyl-CoA. The first half-reaction catalyzed by biotin carboxylase, is an ATP-dependent carboxylation of biotin, which is covalently attached to biotin carboxyl carrier protein. The second half-reaction, catalyzed by carboxyl transferase, transfers the activated carboxyl group from carboxy-biotin to acetyl-CoA to form malonyl-CoA. Interactions among the components of the functional complex are weak, and upon cell lysis, they readily dissociate into stable carboxyl transferase and biotin carboxylase components plus a metastable complex of a biotin carboxylase dimer with four biotin carboxyl carrier protein molecules. Heterododecamer P0ABD8 CPX-3206 Acetyl-CoA carboxylase complex ACC complex|Biotin-dependent acetyl-coenzyme A carboxylase complex|ACCase complex CHEBI:15956(1)|P0ABD8(1)|CHEBI:15956(1)|CHEBI:15956(1)|P24182(2)|P0A9Q5(1)|CHEBI:29105(1)|P0ABD8(1)|P0ABD8(1)|CHEBI:29105(1)|P0A9Q5(1)|P0ABD5(2)|CHEBI:15956(1)|P0ABD8(1)|P24182(2) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Biotin-dependent, multifunctional enzyme that catalyzes the first committed step in fatty acid synthesis.The overall reaction is the biotin-dependent carboxylation of acetyl-CoA to form malonyl-CoA. The first half-reaction catalyzed by biotin carboxylase, is an ATP-dependent carboxylation of biotin, which is covalently attached to biotin carboxyl carrier protein. The second half-reaction, catalyzed by carboxyl transferase, transfers the activated carboxyl group from carboxy-biotin to acetyl-CoA to form malonyl-CoA. Interactions among the components of the functional complex are weak, and upon cell lysis, they readily dissociate into stable carboxyl transferase and biotin carboxylase components plus a metastable complex of a biotin carboxylase dimer with four biotin carboxyl carrier protein molecules. Heterododecamer P0ABD8 CPX-3206 Acetyl-CoA carboxylase complex ACC complex|Biotin-dependent acetyl-coenzyme A carboxylase complex|ACCase complex CHEBI:15956(1)|P0ABD8(1)|CHEBI:15956(1)|CHEBI:15956(1)|P24182(2)|P0A9Q5(1)|CHEBI:29105(1)|P0ABD8(1)|P0ABD8(1)|CHEBI:29105(1)|P0A9Q5(1)|P0ABD5(2)|CHEBI:15956(1)|P0ABD8(1)|P24182(2) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Biotin-dependent, multifunctional enzyme that catalyzes the first committed step in fatty acid synthesis.The overall reaction is the biotin-dependent carboxylation of acetyl-CoA to form malonyl-CoA. The first half-reaction catalyzed by biotin carboxylase, is an ATP-dependent carboxylation of biotin, which is covalently attached to biotin carboxyl carrier protein. The second half-reaction, catalyzed by carboxyl transferase, transfers the activated carboxyl group from carboxy-biotin to acetyl-CoA to form malonyl-CoA. Interactions among the components of the functional complex are weak, and upon cell lysis, they readily dissociate into stable carboxyl transferase and biotin carboxylase components plus a metastable complex of a biotin carboxylase dimer with four biotin carboxyl carrier protein molecules. Heterododecamer P0ABD8 CPX-3206 Acetyl-CoA carboxylase complex ACC complex|Biotin-dependent acetyl-coenzyme A carboxylase complex|ACCase complex CHEBI:15956(1)|P0ABD8(1)|CHEBI:15956(1)|CHEBI:15956(1)|P24182(2)|P0A9Q5(1)|CHEBI:29105(1)|P0ABD8(1)|P0ABD8(1)|CHEBI:29105(1)|P0A9Q5(1)|P0ABD5(2)|CHEBI:15956(1)|P0ABD8(1)|P24182(2) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Biotin-dependent, multifunctional enzyme that catalyzes the first committed step in fatty acid synthesis.The overall reaction is the biotin-dependent carboxylation of acetyl-CoA to form malonyl-CoA. The first half-reaction catalyzed by biotin carboxylase, is an ATP-dependent carboxylation of biotin, which is covalently attached to biotin carboxyl carrier protein. The second half-reaction, catalyzed by carboxyl transferase, transfers the activated carboxyl group from carboxy-biotin to acetyl-CoA to form malonyl-CoA. Interactions among the components of the functional complex are weak, and upon cell lysis, they readily dissociate into stable carboxyl transferase and biotin carboxylase components plus a metastable complex of a biotin carboxylase dimer with four biotin carboxyl carrier protein molecules. Heterododecamer P0ABD8 CPX-3206 Acetyl-CoA carboxylase complex ACC complex|Biotin-dependent acetyl-coenzyme A carboxylase complex|ACCase complex CHEBI:15956(1)|P0ABD8(1)|CHEBI:15956(1)|CHEBI:15956(1)|P24182(2)|P0A9Q5(1)|CHEBI:29105(1)|P0ABD8(1)|P0ABD8(1)|CHEBI:29105(1)|P0A9Q5(1)|P0ABD5(2)|CHEBI:15956(1)|P0ABD8(1)|P24182(2) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Biotin-dependent, multifunctional enzyme that catalyzes the first committed step in fatty acid synthesis.The overall reaction is the biotin-dependent carboxylation of acetyl-CoA to form malonyl-CoA. The first half-reaction catalyzed by biotin carboxylase, is an ATP-dependent carboxylation of biotin, which is covalently attached to biotin carboxyl carrier protein. The second half-reaction, catalyzed by carboxyl transferase, transfers the activated carboxyl group from carboxy-biotin to acetyl-CoA to form malonyl-CoA. Interactions among the components of the functional complex are weak, and upon cell lysis, they readily dissociate into stable carboxyl transferase and biotin carboxylase components plus a metastable complex of a biotin carboxylase dimer with four biotin carboxyl carrier protein molecules. Heterododecamer P0ABJ1 CPX-2102 Cytochrome o ubiquinol oxidase complex ubiquinol:O2 oxidoreductase (H+-transporting)|ubiquinol oxidase|ubiquinol oxidase (H+-transporting)|cytochrome bb3 oxidase|cytochrome bo oxidase|cytochrome bd-I oxidase CHEBI:49637(2)|CHEBI:25805(1)|P0ABI8(1)|P0ABJ6(1)|CHEBI:17976(2)|P0ABJ1(1)|P0ABJ3(1)|CHEBI:24480(1)|CHEBI:28694(1)|CHEBI:26355(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-8697873 A protein complex integral to the bacterial electron transport chain. Electrons are donated by the oxidation of ubiquinol to ubiquinone, transferred to a slow-spinning heme b and subsequently accepted by a binuclear centre consisting of a heme o3 and a copper ion. In the process, the ubiquinol oxidase functions as a proton pump creating a transmembrane electrochemical gradient as 4 hydrogen ions are pumped through the membrane into the periplasmic space while 1/2 O2 molecule is oxidized to water. The electron transport happens exclusively in subunit I (cyoB). Ubiquinol oxidase is the final electron acceptor in the bacterial respiratory chain and thought to possess one of the most important functions in the cellular system due to its anti-oxidant properties. Heteroteramer with two heme units (b and O) cofactors and a copper ion as cofactor. All four subunits are transmembrane spanning from the cytoplasm to the periplasm. It is not known exactly where ubiquinol binds but it is most likely subunit I. Heterotetramer P0ABJ9 CPX-268 Cytochrome bd-I ubiquinol oxidase complex Cytochrome bd-I ubiquinol oxidase|Cytochrome bd-II oxidase P56100(0)|CHEBI:26355(0)|CHEBI:26355(0)|P0ABK2(0)|P0ABJ9(0)|CHEBI:29034(0)|CHEBI:62811(0) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-9258537 A protein complex integral to the bacterial electron transport chain. Electrons are donated by the oxidation of ubiquinol to ubiquinone and used to reduce molecular oxygen, generating a proton motive force using protons and electrons from opposite sides of the membrane to generate water. The oxidase contains three non-covalently bound hemes as cofactors, namely heme b558 functioning as electron acceptor for ubiquinol and hemes b595 and d forming a di-nuclear center to bind and reduce oxygen. The di-heme center is located at the interface of cydA and cydB, cydX may stabilize the di-heme center or it may play a role in its assembly. - P0ABK5 CPX-3742 cysEK cysteine synthase complex CSC|SAT-OASS complex CHEBI:597326(6)|P0A9D4(6)|P0ABK5(4) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-20730165 Catalyzes the final steps in cysteine biosynthesis. The complex is comprised of the two enzymes that catalyze the final steps in cysteine biosynthesis. Serine acetyltransferase (CysE) catalyzes an acyl transfer from acetyl-CoA to L-Ser using a random-order kinetic mechanism to form O-acetyl-l-serine (OAS). OAS allosterically regulates CysB (P0A9F3), a transcriptional activator of the cysteine regulon, up-regulating CysB expression by binding to and preventing CysB from binding to its own promoter, where it inhibits transcription. OAS also regulates the balance of the bound and free forms of CysE and CysK by binding to and dissociating the complex. CysK a pyridoxal 5â€?phosphate (PLP)-dependent enzyme, appears to be inactive in the complex, but when active, displaces the acetoxy group from OAS with bisulfide to yield L-Cys. Dissociation therefore stimulates both OAS consumption and cysteine synthesis. CysE (a dimer of homotrimers) binds a maximum of two molecules of CysK (a dimer) in an interaction believed to involve docking of the C terminus from a protein in CysE trimer into an CysK active site. This interaction inactivates CysK catalysis and also prevents further binding to the trimer. Heterodecamer P0ABT2 CPX-1948 DnaA-Dps complex - chebi:4705(0)|P03004(0)|P03004(0)|P0ABT2(12) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-6402600 Complex formation reduces replication initiation on oriC under oxidative stress conditions allowing DNA repair to proceed, prior to new rounds of replication. The incomplete blockage of replication initiation is thought to produce genetic variation in the bacterial population. - Hetero-oligomer P0AC41 CPX-1931 Respiratory chain complex II SQR|Succinate-quinone oxidoreductase|4 succinate dehydrogenase|Succinate dehydrogenase (ubiquinone)|Respiratory chain complex II|Complex II|Succinate:ubiquinone oxidoreductase|CII|Fumarate reductase complex|Menaquinol: fumarate oxidoreductase|Succinic dehydrogenase CHEBI:36141(1)|CHEBI:47402(1)|CHEBI:33725(1)|CHEBI:33739(1)|CHEBI:51381(3)|CHEBI:30413(1)|P0AC41(3)|P07014(3)|P0AC44(3)|P69054(3)|CHEBI:16238(0) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-6395668 Key enzyme linking the Krebs cycle with the respiratory chain in aerobic respiration: Catalyzes the oxidation of succinate to fumarate and the reduction of quinone to quinol. Electrons flow from the FAD-bound succinate through the Fe-S clusters to a b556 heme. Electrons ultimately reduce quinone to quinol in the membrane bound part of the enzyme. Under most conditions the electrons are used to reduce oxygen, allowing ATP synthesis. Member of the Complex II family. The functionally inverse complex found in anaerobic respiration is the QFR complex (CPX-1967). Trimeric tetramer: SDH is composed of a FAD-containing catalytic subunit dhsa, a Fe-S cluster-containing electron transfer subunit dhsb and the heme-binding subunits dhsc and dhsd. Succinate binds to the dhsa-bound FAD cofactor and quinone binds to the interface of dhsb-dhsc-dhsd situated in the plasma membrane. Dhsa and dhsb comprise the cytoplasmic, soluble subunits of the complex, whereas dhsc and dhsd make up the hydrophobic, trans-membrane subunits. Heteroduodecamer P0AC47 CPX-1967 Plasma membrane fumarate reductase complex QFR complex|quinol-fumarate reductase respiratory complex|fumarate reductase complex CHEBI:17594(2)|CHEBI:16238(1)|CHEBI:33725(1)|CHEBI:47402(1)|CHEBI:33739(1)|P00363(1)|P0AC47(1)|P0A8Q3(1)|P0A8Q0(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-1033003 Catalyzes the terminal step of anaerobic respiration. Electrons are donated to membrane-bound subunits FrdC and FrdD by 2 quinol (hydroquinone) molecules and transferred to a flavin adenine nucleotide (FAD, covalently-bound to subunit FrdA) through three distinct Fe-S clusters (within subunit FrdB). Ultimately, the electrons are used to reduce FAD-bound fumarate to succinate. Electrons can also be transported in the opposite direction where they are donated by succinate and ultimately reduce quinone to quinol. Member of the Complex II family. The functionally inverse complex found in aerobic respiration is the SQR complex (CPX-1931). QFR is composed of a FAD-binding catalytic subunit FrdA, a Fe-S cluster-containing electron transfer subunit FrdB and the transmembrane subunits FrdC and FrdD. Fumarate binds to the FrdA-bound FAD cofactor and the quinol molecules bind to 2 binding sites in the FrdC-FrdD dimer interface. FrdA and FrdB comprise the cytoplasmic, soluble, subunits of the complex, whereas FrdC and FrdD make up the hydrophobic, transmembrane subunits. Heterotetramer P0ACD8 CPX-281 Hydrogenase-1 complex [NiFe] hydrogenase 1 complex|Hyd1 complex|[NiFe]-hydrogenase/cytochrome b complex|H2ase 1 complex CHEBI:49786(1)|CHEBI:49786(1)|CHEBI:30413(2)|CHEBI:49883(1)|CHEBI:49883(2)|CHEBI:21137(1)|CHEBI:21137(1)|P69739(1)|P0ACD8(1)|P0AAM1(1)|P69739(1)|P0ACD8(1)|CHEBI:49883(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-16028656 Catalyzes the reversible oxidation of hydrogen (H2) to protons and electrons. Maximally produced during fermentation and under various types of stress such as carbon and phosphate starvation, osmotic up shift, and stationary phase conditions. Hydrogenase-1 is oxygen tolerant and contains the special proximal (relative to the active site) [Fe4S3] cluster that can rapidly undergo two successive one-electron oxidations within a narrow potential range. The additional two electrons required to reduce the attacking O2 to two water molecules can originate from either the two-electron oxidation of Ni(I) to Ni(III) or the one-electron oxidation of Ni(II) to Ni(III) at the active site, the latter coupled to the one-electron oxidation of the [Fe4S4] medial cluster. Anchored to the periplasmic side of the cytoplasmic membrane by both the hyaA C-terminal transmembrane alpha helix and an integral membrane b-type cytochrome. Heteropentamer P0ACD8 CPX-281 Hydrogenase-1 complex [NiFe] hydrogenase 1 complex|Hyd1 complex|[NiFe]-hydrogenase/cytochrome b complex|H2ase 1 complex CHEBI:49786(1)|CHEBI:49786(1)|CHEBI:30413(2)|CHEBI:49883(1)|CHEBI:49883(2)|CHEBI:21137(1)|CHEBI:21137(1)|P69739(1)|P0ACD8(1)|P0AAM1(1)|P69739(1)|P0ACD8(1)|CHEBI:49883(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-16028656 Catalyzes the reversible oxidation of hydrogen (H2) to protons and electrons. Maximally produced during fermentation and under various types of stress such as carbon and phosphate starvation, osmotic up shift, and stationary phase conditions. Hydrogenase-1 is oxygen tolerant and contains the special proximal (relative to the active site) [Fe4S3] cluster that can rapidly undergo two successive one-electron oxidations within a narrow potential range. The additional two electrons required to reduce the attacking O2 to two water molecules can originate from either the two-electron oxidation of Ni(I) to Ni(III) or the one-electron oxidation of Ni(II) to Ni(III) at the active site, the latter coupled to the one-electron oxidation of the [Fe4S4] medial cluster. Anchored to the periplasmic side of the cytoplasmic membrane by both the hyaA C-terminal transmembrane alpha helix and an integral membrane b-type cytochrome. Heteropentamer P0ACF0 CPX-1958 HU complex HUab-DNA-complex|HUalpha/beta-DNA-complex|HU-DNA complex|HU-DNA binding complex|HU-DNA bending complex|dbha-dbhb complex P0ACF0(1)|P0ACF4(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-15626665 Histone-like DNA-binding complex that is capable of wrapping DNA forming nucleosome-like structures. May play a role in replication initiation, transcription, DNA repair (esp. site-specific recombination) and may protect DNA against UV or gamma radiation. Alpha knock-out mutants cause uncoordinated replication initiation. Preferentially binds strongly bent, kinked or distorted DNA such as that found in damaged DNA. In cooperation with topoisomerase I the complex generates negative supercoiling of the bacterial chromosome. Also binds to DnaA during replication initiation as does the alpha homodimer (CPX-1959). The alpha/beta heterodimer is predominantly present during the transition phase, end of exponential phase and stationary phase. Forms a heterodimer from the alpha and beta subunits. Binds to double-stranded DNA. Subsequently, through coorporative binding, the dimers can form octamers along the DNA strand. Heterodimer P0ACF0 CPX-1959 HU complex variant 1 HUa-DNA-complex|HUalpha-DNA-complex|HUalpha-DNA binding complex|HUalpha-DNA bending complex|HUa-DNA binding complex|HUa-DNA bending complex|HUalpha complex|dbha dimer P0ACF0(2) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-6678706 Histone-like DNA-binding complex that is capable of wrapping DNA forming nucleosome-like structures. May play a role in replication initiation, transcription, DNA repair (esp. site-specific recombiation) and may protect DNA against UV- or gamma-radiation. Knock-out mutants cause uncoordinated replication initiation. Preferentially binds distorted DNA such as that is found in damaged DNA. In cooperation with topoisomerase I the complex generates negative supercoiling of the bacterial chromosome. Also binds to DnaA during replication initiation as does the heterodimer (CPX-1958). The alpha homodimer is predominantly present in the early log phase. DNA-binding is both, topology- or structural-dependent and sequence-specific. Homodimer. Binds to double-stranded DNA. Homodimer P0ACF0 CPX-1962 DnaA-HU complex variant 1 DnaA-HUa-DNA-complex|DnaA-HUalpha-DNA-complex|DnaA-DbhA-DNA complex P0ACF0(2)|P03004(0)|chebi:4705(0) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-6530560 HU dimers (alpha homodimers as well as alpha-beta dimers [CPX-1958]) are essential proteins during the DnaA-dependent initiation of replication. They facilitate DnaA oligomerization and proper timing of initiation of replication. HU forms a homodimer (CPX-1959) that binds to the DnaA oligomer (CPX-1943) at the replication origin (oriC). - P0ACF0 CPX-1961 DnaA-HU complex DnaA-HUab-DNA-complex|DnaA-HUalpha/beta-DNA-complex|DnaA-HU-DNA complex|DnaA-DbhA-DbhB-DNA complex P0ACF0(1)|chebi:4705(0)|P03004(0)|P0ACF4(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-6479010 HU dimers (alpha-beta dimers as well as alpha homodimers [CPX-1959]) are essential proteins during the DnaA-dependent initiation of replication. They facilitate DnaA oligomerization and proper timing of initiation of replication. HU forms a heterodimer (CPX-1958) that binds to the DnaA oligomer (CPX-1943) at the oriC. - P0ACF4 CPX-1958 HU complex HUab-DNA-complex|HUalpha/beta-DNA-complex|HU-DNA complex|HU-DNA binding complex|HU-DNA bending complex|dbha-dbhb complex P0ACF0(1)|P0ACF4(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-15626665 Histone-like DNA-binding complex that is capable of wrapping DNA forming nucleosome-like structures. May play a role in replication initiation, transcription, DNA repair (esp. site-specific recombination) and may protect DNA against UV or gamma radiation. Alpha knock-out mutants cause uncoordinated replication initiation. Preferentially binds strongly bent, kinked or distorted DNA such as that found in damaged DNA. In cooperation with topoisomerase I the complex generates negative supercoiling of the bacterial chromosome. Also binds to DnaA during replication initiation as does the alpha homodimer (CPX-1959). The alpha/beta heterodimer is predominantly present during the transition phase, end of exponential phase and stationary phase. Forms a heterodimer from the alpha and beta subunits. Binds to double-stranded DNA. Subsequently, through coorporative binding, the dimers can form octamers along the DNA strand. Heterodimer P0ACF4 CPX-1960 HU complex variant 2 HUb-DNA-complex|HUbeta-DNA-complex|dbhb dimer P0ACF4(2) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-6678759 Histone-like DNA-binding complex. Preferentially binds cruciform DNA in comparison to the alpha/beta heterodimer (CPX-1958) or alpha homodimer (CPX-1959) that bind to several forms of bent, kinked or damaged DNA. The precise role for the beta homodimer is unknown as knock-out mutants produce no measurable phenotypes. Homodimer. Binds to double-stranded DNA. Homodimer P0ACF4 CPX-1961 DnaA-HU complex DnaA-HUab-DNA-complex|DnaA-HUalpha/beta-DNA-complex|DnaA-HU-DNA complex|DnaA-DbhA-DbhB-DNA complex P0ACF0(1)|chebi:4705(0)|P03004(0)|P0ACF4(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-6479010 HU dimers (alpha-beta dimers as well as alpha homodimers [CPX-1959]) are essential proteins during the DnaA-dependent initiation of replication. They facilitate DnaA oligomerization and proper timing of initiation of replication. HU forms a heterodimer (CPX-1958) that binds to the DnaA oligomer (CPX-1943) at the oriC. - P0ACF8 CPX-1965 H-NS complex, dimeric DNA-binding protein H-NS|histone-like protein H-NS|nucleoid protein H-NS|nucleoid-associated transcriptional repressor H-NS|histone-like protein HLP-II|Protein B1|Protein H1 P0ACF8(2) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-6692727 Involved in bacterial nucleoid condensation and regulation of global gene expression by directly binding to promoter regions, regulation is generally negative although examples of positive regulation are known. Repression of transcription is mediated by cooperative spreading along the DNA (DNA stiffening) and by creating looped structures through formation of DNA-protein-DNA bridges. Recognises both structural and sequence-specific motifs in double-stranded DNA and binds preferably to bent DNA. Whilst dimerization is essential for its transcriptional repressor activity it may be the tetrameric form is more commonly found in vivo. Tetramerization is environmentally dependent and decreases under low ionic strength or temperature conditions. This environmental-dependency of the H-NS tetramer may allow for gene regulation under extreme conditions. Homodimer, also forms homotetramer (CPX-1966) and possibly higher order oligomers. Dimer: MW ~ 30 kD Residue Leu30 appears to be essential for dimerization. NMR data suggests that the 2 central DNA binding regions are very flexible which supports the idea that H-NS has a strong binding affinity for bent DNA. Homodimer P0ACF8 CPX-1966 H-NS complex, tetrameric DNA-binding protein H-NS|histone-like protein H-NS|nucleoid protein H-NS|nucleoid-associated transcriptional repressor H-NS|histone-like protein HLP-II|Protein B1|Protein H1 P0ACF8(4) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-6726389 Involved in bacterial nucleoid condensation and regulation of global gene expression by directly binding to promoter regions, regulation is generally negative although examples of positive regulation are known. Repression of transcription is mediated by cooperative spreading along the DNA (DNA stiffening) and by creating looped structures through formation of DNA-protein-DNA bridges. Recognises both structural and sequence-specific motifs in double-stranded DNA and binds preferably to bent DNA. Whilst dimerization is essential for its transcriptional repressor activity it may be the tetrameric form is more commonly found in vivo. Tetramerization is environmentally dependent and decreases under low ionic strength or temperature conditions. This environmental-dependency of the H-NS tetramer may allow for gene regulation under extreme conditions.the H-NS tetramer may allow for gene regulation under extreme conditions. Homotetramer, also forms homodimer (CPX-1965) and possibly higher order oligomers. Dimer: MW ~ 30 kD Residue L30 appears to be essential for dimerization. NMR data suggests that the 2 central DNA binding regions are very flexible lacking a lot of structure which supports the idea that H-NS has a strong binding affinity for bent DNA. Homotetramer P0ACF8 CPX-1979 H-NS-Hha transcription factor complex HNS-Hha complex P0ACF8(2)|P0ACE3(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-6956761 Functions as transcription factor that negatively regulates a range of genes, in particular those acquired by horizontal transfer. Hha forms a heterotrimer with the H-NS homodimer (CPX-1965). Asp-48 of HhA and Arg-12 of H-HS are essential binding residues for the complex. Heterotrimer P0ACF8 CPX-1980 H-NS-Cnu transcription factor complex HNS-Cnu complex|H-NS-YdgT complex|HNS-YdgT complex P64467(1)|P0ACF8(2) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-6956801 Functions as a transcription factor that negatively regulates a range of bacterial genes. May modulate filamentous growth by antagonizing the binding of dicA (P06966) to a putative operator sequence on its own gene promoter. Cnu forms a heterotrimer with the H-NS homodimer (CPX-1965). Asp-44 of Cnu is an essential binding residue for the complex. Heterotrimer P0ADY3 CPX-3807 50S large ribosomal subunit 50S subunit P0A7P5(1)|P0A7N1(1)|URS000002D309_83333(1)|URS00005B2216_83333(1)|P0A7Q6(1)|P02413(1)|P0A7Q1(1)|P0AG48(1)|P0AG51(1)|P0AG44(1)|P0AA10(1)|P0A7R1(1)|P0A7M2(1)|P0C018(1)|P0A7N4(1)|P0A7M6(1)|P0A7N9(1)|P0A7K6(1)|P68919(1)|P0ADY3(1)|P60438(1)|P60624(1)|P0ADY7(1)|P0ADZ0(1)|P0A7M9(1)|P0A7L3(1)|P0A7L8(1)|P0A7J7(1)|P0A7L0(1)|P0A7J3(1)|P61175(1)|P60422(1)|P60723(1)|P0AG55(1)|P0A7K2(4)|P62399(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit (CPX-3802) which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 30S subunit is responsible for the catalytic activity of the ribosome, the peptidyltransferase activity required to catalyze peptide bond formation. rplL forms dimers with an elongated shape. Two dimers associate with a copy of rplJ to form part of the L8 ribosomal stalk. The ribosomal stalk helps the ribosome interact with GTP-bound translation factors. Hetero39-mer P0ADY7 CPX-3807 50S large ribosomal subunit 50S subunit P0A7P5(1)|P0A7N1(1)|URS000002D309_83333(1)|URS00005B2216_83333(1)|P0A7Q6(1)|P02413(1)|P0A7Q1(1)|P0AG48(1)|P0AG51(1)|P0AG44(1)|P0AA10(1)|P0A7R1(1)|P0A7M2(1)|P0C018(1)|P0A7N4(1)|P0A7M6(1)|P0A7N9(1)|P0A7K6(1)|P68919(1)|P0ADY3(1)|P60438(1)|P60624(1)|P0ADY7(1)|P0ADZ0(1)|P0A7M9(1)|P0A7L3(1)|P0A7L8(1)|P0A7J7(1)|P0A7L0(1)|P0A7J3(1)|P61175(1)|P60422(1)|P60723(1)|P0AG55(1)|P0A7K2(4)|P62399(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit (CPX-3802) which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 30S subunit is responsible for the catalytic activity of the ribosome, the peptidyltransferase activity required to catalyze peptide bond formation. rplL forms dimers with an elongated shape. Two dimers associate with a copy of rplJ to form part of the L8 ribosomal stalk. The ribosomal stalk helps the ribosome interact with GTP-bound translation factors. Hetero39-mer P0AE67 CPX-1082 Flagellar Motor Switch Complex, CW variant - P0AE67(1)|P06974(0)|P0ABZ1(0)|P15070(0)|CHEBI:18420(0) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Plays a role in chemotaxis, the movement toward or away from chemicals. The flagellar motor of bacteria is a rotary device energized by the membrane ion gradient and the complex is required for the rotation and directional switching of the flagellum and also functions in flagellar assembly. Motor torque is produced at the top of the switch complex, where the fliG C-terminal domain bears several conserved charged residues that interact with charged groups of the stator protein motA (P09348). The conformation of this complex is such that the flagellum rotates in a clockwise (CW) direction, induced by binding of cheY-P to the lower part of the C-ring. cheY-P interacts initially with the N-terminal segment of fliM, which is flexible enough to allow subsequent binding to a site on fliN. Coupled conformational transitions in fliM trigger large displacements of a distant alpha-helix in fliG, involved in stator contacts, inducing the change of the flagellar rotors from counterclocwise (smooth-swimming phenotype) to clockwise rotation (tumbly phenotype). Formed from about 26 copies of fliG, 34 copies of fliM, and more than 100 copies of fliN. The lower part of the switch complex is formed from fliN, organized in doughnut-shaped tetramers that alternate with the fliM C-terminal domains in an array at the membrane distal region of a large drum-shaped feature of approximately 40nM, at the bottom of the basal body - the C-ring. The thinner side-wall of the C-ring, above the fliN/fliM C-terminal array, is formed from the fliM middle domain. fliG is proximal to the membrane and its middle domain interacts with fliM. Phosphoryl-cheY binds fliM with approximately 20-fold higher affinity than non-phosphorylated cheY. Binding measurements suggest that the switch binds many CheY-P molecules, and that several molecules must interact with the switch simultaneously to trigger direction reversal. - P0AE67 CPX-1077 Chemotaxis phosphorelay complex CheA-CheY - CHEBI:18420(1)|P0AE67(1)|P07363(1) ECO:0000353(physical interaction evidence used in manual assertion) - Plays a role in chemotaxis, the movement toward or away from chemicals. The complex is formed to activate cheY protein that then induces the change of the flagellar rotors from counterclocwise to clockwise rotation. cheA interacts with transmembrane chemoreceptors to generate stimulus signals via autophosphorylion of cheA which then serves as a phosphodonor for cheY. The P-cheY generated by this interaction binds to fliM (P06974), the switch component of the flagellar motor. - Heterodimer P0AE67 CPX-1088 Chemotaxis phosphorelay complex CheY-CheZ - CHEBI:18420(1)|CHEBI:18420(1)|P0A9H9(1)|P0AE67(1)|P0AE67(1)|P0A9H9(1) ECO:0000353(physical interaction evidence used in manual assertion) - Plays a role in chemotaxis, the movement toward or away from chemicals. The flagellar motor of bacteria is a rotary device energized by the membrane ion gradient and the complex is required for the rotation and directional switching of the flagellum and also functions in flagellar assembly. Motor torque is produced at the top of the switch complex, where the fliG C-terminal domain bears several conserved charged residues that interact with charged groups of the stator protein motA (P09348). The directionality of the rotation is determined by binding of cheY-P to the lower part of the C-ring which switches the directionality from counter-clockwise to clockwise. The cheY-cheZ complex enhances the dephosphorylation rate of P-cheY. This dephosphorylation reduces the binding of cheY to the switch and ensures rapid locomotor responses to changes in the supply of signaling phosphoryl groups to cheY, thus enabling a continuous response to environmental changes. The side chain of Gln-147 of cheZ inserts into the cheY active site, filling one coordination site of the Mg2+, and rendering the existing mechanism of CheY autodephosphorylation more efficient by positioning a water molecule in the appropriate geometry for nucleophilic attack. Heterotetramer P0AE67 CPX-1088 Chemotaxis phosphorelay complex CheY-CheZ - CHEBI:18420(1)|CHEBI:18420(1)|P0A9H9(1)|P0AE67(1)|P0AE67(1)|P0A9H9(1) ECO:0000353(physical interaction evidence used in manual assertion) - Plays a role in chemotaxis, the movement toward or away from chemicals. The flagellar motor of bacteria is a rotary device energized by the membrane ion gradient and the complex is required for the rotation and directional switching of the flagellum and also functions in flagellar assembly. Motor torque is produced at the top of the switch complex, where the fliG C-terminal domain bears several conserved charged residues that interact with charged groups of the stator protein motA (P09348). The directionality of the rotation is determined by binding of cheY-P to the lower part of the C-ring which switches the directionality from counter-clockwise to clockwise. The cheY-cheZ complex enhances the dephosphorylation rate of P-cheY. This dephosphorylation reduces the binding of cheY to the switch and ensures rapid locomotor responses to changes in the supply of signaling phosphoryl groups to cheY, thus enabling a continuous response to environmental changes. The side chain of Gln-147 of cheZ inserts into the cheY active site, filling one coordination site of the Mg2+, and rendering the existing mechanism of CheY autodephosphorylation more efficient by positioning a water molecule in the appropriate geometry for nucleophilic attack. Heterotetramer P0AEX9 CPX-1932 Maltose transport complex MalE-MalFGK2 complex|maltose transporter|maltose transporter malE-MalFGK2|maltose transporter MalE-MalFGK2 complex|maltose-transporting ATPase|maltose ATP-binding cassette (ABC) transporter complex|ATP phosphohydrolase (maltose-importing) P68187(2)|CHEBI:17306(1)|P02916(1)|P0AEX9(1)|P68183(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-6477279 Transports maltose from the periplasmic space into the cytoplasm through an ATP-dependent transmembrane channel. Maltose binds to malE which attaches to the malFG dimer. Upon release of the maltose into the transmembrane channel, the malK2 dimer binds ATP the hydrolysis of which triggers the release of maltose into the cytoplasm. Consists of periplasmic maltose binding protein MalE (P0AEX9), transmembrane MalF-MalG dimer (P02916-P68183) and cytoplasmic ATPase subunit MalK dimer (P68187). Heteropentamer P0AFC7 CPX-243 Respiratory chain complex I NADH:ubiquinone oxidoreductase|NDH-I|NADH-quinone oxidoreductase|NADH:quinone oxidoreductase|Respiratory complex I CHEBI:64607(0)|CHEBI:64607(0)|P0AFE4(0)|P0AFD6(0)|P0AFD4(0)|P33602(0)|P31979(0)|P0AFD1(0)|P33599(0)|P0AFC7(0)|CHEBI:49601(0)|CHEBI:64607(0)|CHEBI:49601(0)|CHEBI:64607(0)|CHEBI:58210(0)|P0AFF0(0)|P0AFE8(0)|P33607(0)|P0AFE0(0)|P0AFC3(0) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Catalyses the first step of electron transport by the oxidation of NADH, thus providing two electrons for the reduction of ubiquinone. Electron transfer is coupled with the translocation of protons across the membrane, generating a proton motive force. Preferred NADH dehydrogenase under anaerobic conditions. L-shaped complex consisting of a peripheral arm and a membrane arm. Subunits NuoB, CD, E, F, and G constitute the peripheral sector of the complex, subunits NuoA, H, I, J, K, L, M, N constitute the membrane sector. - P0AFD6 CPX-243 Respiratory chain complex I NADH:ubiquinone oxidoreductase|NDH-I|NADH-quinone oxidoreductase|NADH:quinone oxidoreductase|Respiratory complex I CHEBI:64607(0)|CHEBI:64607(0)|P0AFE4(0)|P0AFD6(0)|P0AFD4(0)|P33602(0)|P31979(0)|P0AFD1(0)|P33599(0)|P0AFC7(0)|CHEBI:49601(0)|CHEBI:64607(0)|CHEBI:49601(0)|CHEBI:64607(0)|CHEBI:58210(0)|P0AFF0(0)|P0AFE8(0)|P33607(0)|P0AFE0(0)|P0AFC3(0) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Catalyses the first step of electron transport by the oxidation of NADH, thus providing two electrons for the reduction of ubiquinone. Electron transfer is coupled with the translocation of protons across the membrane, generating a proton motive force. Preferred NADH dehydrogenase under anaerobic conditions. L-shaped complex consisting of a peripheral arm and a membrane arm. Subunits NuoB, CD, E, F, and G constitute the peripheral sector of the complex, subunits NuoA, H, I, J, K, L, M, N constitute the membrane sector. - P0AFG6 CPX-3921 2-oxoglutarate dehydrogenase complex alpha-Ketoglutarate dehydrogenase complex|OGDH complex|dihydrolipoamide S-succinyltransferase complex P0A9P0(1)|CHEBI:57692(1)|CHEBI:58937(0)|CHEBI:83088(0)|P0AFG3(12)|P0AFG6(24)|P0A9P0(1)|CHEBI:57692(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Multi-enzyme complex that catalyzes the conversion of 2-oxoglutarate (2-ketoglutarate) to succinyl-CoA and CO2, with the production of NADH, during the citric acid cycle. It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3). 2-oxoglutarate is bound and decarboxylated by sucA, sucB catalyzes the transfer of a succinyl group from the S-succinyldihydrolipoyl moiety to coenzyme A, forming succinyl-CoA and lpdA catalyzes the transfer of electrons to the ultimate acceptor, NAD. sucA and lpdA are recruited through direct interaction with sucB, which is an oligomeric enzyme with structurally distinct domains that are linked by flexible regions of polypeptide chain of 28â€?0 residues that are rich in Ala and Pro. Hetero28-mer P0AFG8 CPX-3943 Pyruvate dehydrogenase complex PDH complex|dihydrolipoyl dehydrogenase complex|PDHC P0A9P0(12)|P0AFG8(24)|P06959(24)|CHEBI:57692(12)|CHEBI:83088(0)|CHEBI:58937(0)|CHEBI:18420(0) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Converts pyruvate to acetyl-CoA and CO2, thus providing a metabolic connection between glycolysis, whose end product is pyruvate, and the tricarboxylic acid cycle, which starts with acetyl-CoA. It contains multiple copies of three enzymatic components, that are encoded by a single operon: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). In anaerobic Escherichia coli, the complex is normally inactive due to inhibition of ldpA by NADH. During aerobic growth, the NADH generated in glycolysis is oxidized and the complex becomes active. Assembled symmetrically around a 24-polypeptide structural core with octahedral symmetry built mainly from catalytic domains in the aceF components, with the peripheral aceE and lpdA components displaced and separated from the core by large distances but tethered to it by flexible linkers non-covalently bound to them. - P0AFM2 CPX-2126 ProVWX complex ATP-binding cassette (ABC) transporter complex ProVWX P0AFM2(0)|P14175(0)|P14176(0) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-8794760 Belongs to the family of ATP-binding cassette (ABC) transporter proteins complexes. It is capable of translocating a wide variety of solutes (e.g. glycine betaine) across the plasma membrane. The proVWX operon is activated under osmotic stress conditions. Putative pentamer. The transmembrane subunit ProW and the cytoplasmic, CBS (cystathionine-beta-synthase) domain-containing ATPase subunit ProV are each thought to be dimeric while the periplasmic binding protein ProX is probably a monomer. - P0AG48 CPX-3807 50S large ribosomal subunit 50S subunit P0A7P5(1)|P0A7N1(1)|URS000002D309_83333(1)|URS00005B2216_83333(1)|P0A7Q6(1)|P02413(1)|P0A7Q1(1)|P0AG48(1)|P0AG51(1)|P0AG44(1)|P0AA10(1)|P0A7R1(1)|P0A7M2(1)|P0C018(1)|P0A7N4(1)|P0A7M6(1)|P0A7N9(1)|P0A7K6(1)|P68919(1)|P0ADY3(1)|P60438(1)|P60624(1)|P0ADY7(1)|P0ADZ0(1)|P0A7M9(1)|P0A7L3(1)|P0A7L8(1)|P0A7J7(1)|P0A7L0(1)|P0A7J3(1)|P61175(1)|P60422(1)|P60723(1)|P0AG55(1)|P0A7K2(4)|P62399(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit (CPX-3802) which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 30S subunit is responsible for the catalytic activity of the ribosome, the peptidyltransferase activity required to catalyze peptide bond formation. rplL forms dimers with an elongated shape. Two dimers associate with a copy of rplJ to form part of the L8 ribosomal stalk. The ribosomal stalk helps the ribosome interact with GTP-bound translation factors. Hetero39-mer P0AG51 CPX-3807 50S large ribosomal subunit 50S subunit P0A7P5(1)|P0A7N1(1)|URS000002D309_83333(1)|URS00005B2216_83333(1)|P0A7Q6(1)|P02413(1)|P0A7Q1(1)|P0AG48(1)|P0AG51(1)|P0AG44(1)|P0AA10(1)|P0A7R1(1)|P0A7M2(1)|P0C018(1)|P0A7N4(1)|P0A7M6(1)|P0A7N9(1)|P0A7K6(1)|P68919(1)|P0ADY3(1)|P60438(1)|P60624(1)|P0ADY7(1)|P0ADZ0(1)|P0A7M9(1)|P0A7L3(1)|P0A7L8(1)|P0A7J7(1)|P0A7L0(1)|P0A7J3(1)|P61175(1)|P60422(1)|P60723(1)|P0AG55(1)|P0A7K2(4)|P62399(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit (CPX-3802) which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 30S subunit is responsible for the catalytic activity of the ribosome, the peptidyltransferase activity required to catalyze peptide bond formation. rplL forms dimers with an elongated shape. Two dimers associate with a copy of rplJ to form part of the L8 ribosomal stalk. The ribosomal stalk helps the ribosome interact with GTP-bound translation factors. Hetero39-mer P0AG55 CPX-3807 50S large ribosomal subunit 50S subunit P0A7P5(1)|P0A7N1(1)|URS000002D309_83333(1)|URS00005B2216_83333(1)|P0A7Q6(1)|P02413(1)|P0A7Q1(1)|P0AG48(1)|P0AG51(1)|P0AG44(1)|P0AA10(1)|P0A7R1(1)|P0A7M2(1)|P0C018(1)|P0A7N4(1)|P0A7M6(1)|P0A7N9(1)|P0A7K6(1)|P68919(1)|P0ADY3(1)|P60438(1)|P60624(1)|P0ADY7(1)|P0ADZ0(1)|P0A7M9(1)|P0A7L3(1)|P0A7L8(1)|P0A7J7(1)|P0A7L0(1)|P0A7J3(1)|P61175(1)|P60422(1)|P60723(1)|P0AG55(1)|P0A7K2(4)|P62399(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit (CPX-3802) which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 30S subunit is responsible for the catalytic activity of the ribosome, the peptidyltransferase activity required to catalyze peptide bond formation. rplL forms dimers with an elongated shape. Two dimers associate with a copy of rplJ to form part of the L8 ribosomal stalk. The ribosomal stalk helps the ribosome interact with GTP-bound translation factors. Hetero39-mer P0AG63 CPX-3802 30S small ribosomal subunit 30S subunit P68679(1)|URS00005CADE5_83333(1)|P0A7R5(1)|P0A7X3(1)|P0A7T3(1)|P0A7U3(1)|P0A7U7(1)|P0A7V3(1)|P0A7R9(1)|P0A7W7(1)|P0A7T7(1)|P0AG63(1)|P0A7V0(1)|P0ADZ4(1)|P0A7S3(1)|P0A7V8(1)|P0A7W1(1)|P0A7S9(1)|P02359(1)|P0AG67(1)|P02358(1)|P0AG59(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit (CPX-3807) which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 50S subunit acts as the decoding centre of the ribosome which brings mRNA and aminoacylated transfer (t)RNAs together, with the 16S ribosomal (r)RNA being required for the selection of the cognate tRNA. Guides the initiating start codon AUG of mRNA into position by recognizing the Shine-Dalgarno sequence, a complementary binding site about 8 base pairs upstream from the start codon. In order to form the translation complex with the 50S subunit, the 30S subunit must bind the Translation Initiation factor complex (CPX-2244), mRNA, and f-met-tRNA. The mRNA entrance channel is formed mainly by proteins rpsC, rpsD, and rpsE. Hetero22-mer P0AG67 CPX-3802 30S small ribosomal subunit 30S subunit P68679(1)|URS00005CADE5_83333(1)|P0A7R5(1)|P0A7X3(1)|P0A7T3(1)|P0A7U3(1)|P0A7U7(1)|P0A7V3(1)|P0A7R9(1)|P0A7W7(1)|P0A7T7(1)|P0AG63(1)|P0A7V0(1)|P0ADZ4(1)|P0A7S3(1)|P0A7V8(1)|P0A7W1(1)|P0A7S9(1)|P02359(1)|P0AG67(1)|P02358(1)|P0AG59(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit (CPX-3807) which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 50S subunit acts as the decoding centre of the ribosome which brings mRNA and aminoacylated transfer (t)RNAs together, with the 16S ribosomal (r)RNA being required for the selection of the cognate tRNA. Guides the initiating start codon AUG of mRNA into position by recognizing the Shine-Dalgarno sequence, a complementary binding site about 8 base pairs upstream from the start codon. In order to form the translation complex with the 50S subunit, the 30S subunit must bind the Translation Initiation factor complex (CPX-2244), mRNA, and f-met-tRNA. The mRNA entrance channel is formed mainly by proteins rpsC, rpsD, and rpsE. Hetero22-mer P0AGA2 CPX-1095 Holo-translocon SecYEG-SecDF-YajC-YidC complex HTL complex P0ADZ7(1)|P0AGA2(1)|P0AG93(1)|P0AG90(1)|P25714(1)|P0AG99(1)|P0AG96(1) ECO:0000353(physical interaction evidence used in manual assertion) - Functions in both protein secretion to the trans side of the plasma membrane and insertion of membrane proteins into the lipid bilayer. The HTL complex is more proficient in cotranslational membrane protein insertion compared with SecYEG (CPX-1096) alone and the post-translational secretion of a beta-barreled outer-membrane protein driven by secA and ATP becomes much more dependent on the proton-motive force than is the case for SecYEG. The yidC periplasmic and secD periplasmic region P1-head domains are positioned to interact with translocation substrates preventing backsliding of the polypeptide through the translocation channel. The SecYEG translocon forms a central pore through which hydrophilic polypeptides are transported, otherwise closed by a girdle of hydrophobic residues and a short helix plug. A lateral gate is formed between SecY transmembrane helices through which transmembrane helices partition into the lipid bilayer. yidC is required to facilitate this passage from the lateral gate and for the subsequent folding and assembly of inner membrane-proteins and complexes. The ancillary SecDF sub-complex stimulates protein translocation through SecYEG8 assisted by the transmembrane proton-motive force. The periplasmic domain of SecD consists of a P1-head and a P1-base domain, which are thought to contact the substrate and move in response to proton translocation; thereby facilitating the passage of polypeptides across the membrane Heteroheptamer P0AGA2 CPX-1096 Protein-conducting channel SecYEG complex Sec complex|SecYEG preprotein translocase complex P0AGA2(2)|P0AG99(2)|P0AG96(2) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-15855164 Functions in both protein secretion to the trans side of the plasma membrane and insertion of membrane proteins into the lipid bilayer. Associates with the motor ATPase SecA, which drives post-translational translocation of pre-proteins across the membrane.Membrane proteins are targeted to the membrane co-translationally by the signal recognition particle (SRP) associating with its receptor at the cytosolic surface. The ribosome nascent chain complex is then passed onto the dimeric SecYEG complex and the nascent membrane protein is threaded through the protein channel and into the bilayer via a lateral gate. Also forms a holo-translocon super-complex comprising of the SecYEG core complex, the accessory sub-complex SecDF–YajC and YidC. Forms an hourglass-shaped structure composed of 10 transmembrane helices of SecY hinged by SecE on one side, allowing for a clamp-like action that opens and closes the lateral gate region formed between SecY transmembrane helices on the side opposite the hinge. Signal-anchor sequences insert into the lateral gate region of the channel, allowing for the subsequent release of membrane proteins into the lipid bilayer. The channel complex also contains a constriction pore at its center as well as a small helical plug domain that relocates to the channel exterior to open a path for the translocation of secretory proteins across the membrane. Translocating preproteins associate with dimeric SecYEG but the dimer appears to readily dissociate into a monomeric form. Heterohexamer P0AGE9 CPX-1092 Succinyl-CoA synthetase - P0A836(2)|P0AGE9(2)|CHEBI:18420(2) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-1770945 Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. It catalyzes the reversible interchange of purine nucleoside diphosphate, succinyl-CoA and phosphate with purine nucleoside triphosphate, succinate, and CoA via a phosphorylated histidine intermediate. The alpha subunit (sucC) of the enzyme binds the substrates CoA and phosphate. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate. During catalysis the histidine residue of alpha subunit (His-246) is transiently phosphorylated. Heterotetramer P0C018 CPX-3807 50S large ribosomal subunit 50S subunit P0A7P5(1)|P0A7N1(1)|URS000002D309_83333(1)|URS00005B2216_83333(1)|P0A7Q6(1)|P02413(1)|P0A7Q1(1)|P0AG48(1)|P0AG51(1)|P0AG44(1)|P0AA10(1)|P0A7R1(1)|P0A7M2(1)|P0C018(1)|P0A7N4(1)|P0A7M6(1)|P0A7N9(1)|P0A7K6(1)|P68919(1)|P0ADY3(1)|P60438(1)|P60624(1)|P0ADY7(1)|P0ADZ0(1)|P0A7M9(1)|P0A7L3(1)|P0A7L8(1)|P0A7J7(1)|P0A7L0(1)|P0A7J3(1)|P61175(1)|P60422(1)|P60723(1)|P0AG55(1)|P0A7K2(4)|P62399(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit (CPX-3802) which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 30S subunit is responsible for the catalytic activity of the ribosome, the peptidyltransferase activity required to catalyze peptide bond formation. rplL forms dimers with an elongated shape. Two dimers associate with a copy of rplJ to form part of the L8 ribosomal stalk. The ribosomal stalk helps the ribosome interact with GTP-bound translation factors. Hetero39-mer P14175 CPX-2126 ProVWX complex ATP-binding cassette (ABC) transporter complex ProVWX P0AFM2(0)|P14175(0)|P14176(0) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-8794760 Belongs to the family of ATP-binding cassette (ABC) transporter proteins complexes. It is capable of translocating a wide variety of solutes (e.g. glycine betaine) across the plasma membrane. The proVWX operon is activated under osmotic stress conditions. Putative pentamer. The transmembrane subunit ProW and the cytoplasmic, CBS (cystathionine-beta-synthase) domain-containing ATPase subunit ProV are each thought to be dimeric while the periplasmic binding protein ProX is probably a monomer. - P17315 CPX-3577 Ferric-catecholate outer membrane transporter complex Iron (III) hydroxamate ABC transporter|Colicin I receptor complex P17315(1)|P0ABU7(6)|P0ABV2(3)|P02929(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - A member of the TonB-dependent transporter family (TBDTs) which binds and then transports Fe3+ complexed to linear catecholates, such as dihydroxybenzoyl, across the outer membrane. Catecholate transport requires an outer membrane receptor (cirA), which is relatively specific for its ligand. The ligand-bound receptor then physically interacts with the TonB protein. TBDTs are energy-dependent gated channels that usually transport large metal complexes which cannot fit through porins, and are too scarce to enter by mass-action-driven transport. Energy-dependent uptake through TBDTs requires interaction with TonB in complex with exbB and exbD in the inner membrane, ExbBD. TonB undergoes rapid energized movement driven by ExbBD which harvests the electrochemical force from the electrochemical proton gradient created by the proton gradient across the inner membrane and convert it into rotational motion. Hence, tonB may pull or twist the N-termini of TBDTs to promote transport of substrates into the periplasm. ATP-binding-cassette (ABC) transporters subsequently move the ferric-catecholate (Fe3+) through the periplasm and inner membrane. The complex has also implicated in the uptake of catechol‐substituted cephalosporins and is used by Group B colicins (E. coli‐specific bacteriocins) to bind and cross the outer membrane. The lumen of cirA, a 22-stranded beta-barrel outer membrane protein, is blocked by an N-terminal plug, or cork, domain preventing passive transit of ferric-catecholate. The binding of a ferric-catecholate induces an allosteric rearrangement of the plug domain, releasing a conserved motif, the Ton-box into the periplasmic space, where it forms a 1:1 complex. The transmembrane helix at the N-terminus of TonB forms a complex with exbB and exbD, which form the proton channel that energizes uptake through TonB. Pentameric and hexameric exbB complexes coexist in detergent micelles and within lipid bilayers, and the ratio of the hexamer to the pentamer increases with pH, similar to the pH dependence of the macroscopic channel conductance. This, and the channel volume of the respective assemblies suggests that the pentamer is less active and the hexamer more active. Heteroheptamer P21177 CPX-3964 fadBA fatty acid oxidation complex, aerobic conditions Fatty acid oxidation complex FADA/B|Aerobic fatty acid oxidation complex P21151(2)|P21177(2) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Catalyzes the final step of fatty acid oxidation in the beta-oxidation pathway. The beta-oxidation pathway acts in a cyclic fashion, in which each cycle results in shortening the input acyl-CoA by two carbon atoms to give acetyl-CoA. Produced acetyl-CoA molecules enter the citric acid cycle (Krebs cycle) to be oxidized for energy production. This complex has five separate enzymatic activities including hydration, oxidation and thiolytic cleavage functions. Escherichia coli uses fatty acids as a sole carbon and energy source during aerobic growth. - Heterotetramer P21513 CPX-403 Degradosome RNA degradosome - core component|RNA degradosome|Degradosome P21513(12)|P0A6P9(16)|P05055(12)|P0A8J8(8) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-849044 Key role in mRNA degradation and RNA processing. RNA binds to RnaE, RhlB helicase is necessary to unwind the RNA secondary structures and, once unwound, the 3â€?5â€?decay of the transcripts is ensued by phosphate-dependent PNPase. RNase E bound-enolase may connect cellular metabolic status with post-transcriptional gene regulation and link RNA degradation to glycolytic processes. A dynamic set of minor components of this complex may regulate its function and compartmentalization. Structured as ordered helical elements arranged in a coil. RNase E provides the backbone of the complex and the N-terminus of this enzyme tethers the degradosome to the cytoplasmic membrane. A ratio of four PNPase trimers binds to three RNase E tetramers and eight enolase dimers and eight RhlB helicase N-terminal domains bind to the C-terminal tails of RNase E. Mg2+ ions coordinate the N-terminal domains of RNase E into catalytic tetrameric domains. - P23874 CPX-180 HipBA toxin-antitoxin complex HipA-HipB complex|HipAB complex|HipAB toxin/antitoxin complex|HipAB DNA-binding transcriptional repressor complex|HipBA DNA-binding transcriptional repressor complex|HipAB TA complex P23874(1)|P23873(1)|P23873(1)|P23874(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-10919388 Toxin-antitoxin (TA) complex. TA systems act as effectors of dormancy and persistence and are composed of a toxin, which causes growth arrest by interfering with a vital cellular process, and a cognate antitoxin, which neutralizes the toxin activity during normal growth conditions. Under conditions of stress the antitoxins are selectively degraded, leaving the toxins to exert their toxic effects, leading to growth arrest and dormancy. Type II TA complexes are small protein-protein pairs; under growth conditions, the toxin is bound to the antitoxin, which inhibits its activity. Both the antitoxin and, in most cases, the TA complex bind the TA promoter to repress transcription. Under stress conditions, cellular proteases such as Lon (P0A9M0) and ClpXP (CPX-3176) are activated that preferentially cleave the antitoxins, freeing the toxins to inhibit growth by inhibiting translation or replication, enabling cells to enter a metabolically dormant state until the stress is removed. Complex formation prevents the protein kinase HipA acting as a persistence factor, inducing multi-drug tolerance by triggering growth arrest. HipA activity is inhibited upon binding to HipB through sequestration to the nucleoid and binding to DNA. HipB and HipAB act as a transcriptional autoregulators of the hipBA operon. In the HipA-HipB-DNA complex, the HipB dimer is sandwiched on each side by one HipA molecule and the complex is formed from noncontiguous regions of both HipA and HipB. Heterotetramer P23874 CPX-180 HipBA toxin-antitoxin complex HipA-HipB complex|HipAB complex|HipAB toxin/antitoxin complex|HipAB DNA-binding transcriptional repressor complex|HipBA DNA-binding transcriptional repressor complex|HipAB TA complex P23874(1)|P23873(1)|P23873(1)|P23874(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-10919388 Toxin-antitoxin (TA) complex. TA systems act as effectors of dormancy and persistence and are composed of a toxin, which causes growth arrest by interfering with a vital cellular process, and a cognate antitoxin, which neutralizes the toxin activity during normal growth conditions. Under conditions of stress the antitoxins are selectively degraded, leaving the toxins to exert their toxic effects, leading to growth arrest and dormancy. Type II TA complexes are small protein-protein pairs; under growth conditions, the toxin is bound to the antitoxin, which inhibits its activity. Both the antitoxin and, in most cases, the TA complex bind the TA promoter to repress transcription. Under stress conditions, cellular proteases such as Lon (P0A9M0) and ClpXP (CPX-3176) are activated that preferentially cleave the antitoxins, freeing the toxins to inhibit growth by inhibiting translation or replication, enabling cells to enter a metabolically dormant state until the stress is removed. Complex formation prevents the protein kinase HipA acting as a persistence factor, inducing multi-drug tolerance by triggering growth arrest. HipA activity is inhibited upon binding to HipB through sequestration to the nucleoid and binding to DNA. HipB and HipAB act as a transcriptional autoregulators of the hipBA operon. In the HipA-HipB-DNA complex, the HipB dimer is sandwiched on each side by one HipA molecule and the complex is formed from noncontiguous regions of both HipA and HipB. Heterotetramer P24182 CPX-3206 Acetyl-CoA carboxylase complex ACC complex|Biotin-dependent acetyl-coenzyme A carboxylase complex|ACCase complex CHEBI:15956(1)|P0ABD8(1)|CHEBI:15956(1)|CHEBI:15956(1)|P24182(2)|P0A9Q5(1)|CHEBI:29105(1)|P0ABD8(1)|P0ABD8(1)|CHEBI:29105(1)|P0A9Q5(1)|P0ABD5(2)|CHEBI:15956(1)|P0ABD8(1)|P24182(2) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Biotin-dependent, multifunctional enzyme that catalyzes the first committed step in fatty acid synthesis.The overall reaction is the biotin-dependent carboxylation of acetyl-CoA to form malonyl-CoA. The first half-reaction catalyzed by biotin carboxylase, is an ATP-dependent carboxylation of biotin, which is covalently attached to biotin carboxyl carrier protein. The second half-reaction, catalyzed by carboxyl transferase, transfers the activated carboxyl group from carboxy-biotin to acetyl-CoA to form malonyl-CoA. Interactions among the components of the functional complex are weak, and upon cell lysis, they readily dissociate into stable carboxyl transferase and biotin carboxylase components plus a metastable complex of a biotin carboxylase dimer with four biotin carboxyl carrier protein molecules. Heterododecamer P24182 CPX-3206 Acetyl-CoA carboxylase complex ACC complex|Biotin-dependent acetyl-coenzyme A carboxylase complex|ACCase complex CHEBI:15956(1)|P0ABD8(1)|CHEBI:15956(1)|CHEBI:15956(1)|P24182(2)|P0A9Q5(1)|CHEBI:29105(1)|P0ABD8(1)|P0ABD8(1)|CHEBI:29105(1)|P0A9Q5(1)|P0ABD5(2)|CHEBI:15956(1)|P0ABD8(1)|P24182(2) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Biotin-dependent, multifunctional enzyme that catalyzes the first committed step in fatty acid synthesis.The overall reaction is the biotin-dependent carboxylation of acetyl-CoA to form malonyl-CoA. The first half-reaction catalyzed by biotin carboxylase, is an ATP-dependent carboxylation of biotin, which is covalently attached to biotin carboxyl carrier protein. The second half-reaction, catalyzed by carboxyl transferase, transfers the activated carboxyl group from carboxy-biotin to acetyl-CoA to form malonyl-CoA. Interactions among the components of the functional complex are weak, and upon cell lysis, they readily dissociate into stable carboxyl transferase and biotin carboxylase components plus a metastable complex of a biotin carboxylase dimer with four biotin carboxyl carrier protein molecules. Heterododecamer P31979 CPX-243 Respiratory chain complex I NADH:ubiquinone oxidoreductase|NDH-I|NADH-quinone oxidoreductase|NADH:quinone oxidoreductase|Respiratory complex I CHEBI:64607(0)|CHEBI:64607(0)|P0AFE4(0)|P0AFD6(0)|P0AFD4(0)|P33602(0)|P31979(0)|P0AFD1(0)|P33599(0)|P0AFC7(0)|CHEBI:49601(0)|CHEBI:64607(0)|CHEBI:49601(0)|CHEBI:64607(0)|CHEBI:58210(0)|P0AFF0(0)|P0AFE8(0)|P33607(0)|P0AFE0(0)|P0AFC3(0) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Catalyses the first step of electron transport by the oxidation of NADH, thus providing two electrons for the reduction of ubiquinone. Electron transfer is coupled with the translocation of protons across the membrane, generating a proton motive force. Preferred NADH dehydrogenase under anaerobic conditions. L-shaped complex consisting of a peripheral arm and a membrane arm. Subunits NuoB, CD, E, F, and G constitute the peripheral sector of the complex, subunits NuoA, H, I, J, K, L, M, N constitute the membrane sector. - P33195 CPX-3949 Glycine cleavage system complex Gycine decarboxylase complex|Glycine cleavage complex|gcvP/T/L/H complex P0A9P0(0)|P27248(0)|P0A6T9(0)|P33195(0)|CHEBI:597326(0)|CHEBI:57692(0)|CHEBI:83088(0) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Multienzyme complex that catalyses the reversible oxidation of glycine, yielding carbon dioxide (CO), ammonia (NH3), 5,10-methylenetetrahydrofolate and a reduced pyridine nucleotide. The 1-carbon units thus generated are used in the synthesis of purines, histidine, thymine, pantothenate, and methionine and in the formylation of the aminoacylated initiator fMet-TRNAfMet required for translation initiation. gcvP binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO2 is released and the remaining methylamine moiety is transferred to the lipoamide cofactor of gcvH, which is bound to the P protein prior to decarboxylation of glycine. gcvT catalyzes the release of NH3 from the methylamine group and transfers the remaining C1 unit to tetrahydrofolate, forming 5,10-methylenetetrahydrofolate. lpdA then oxidizes the lipoic acid component of the H protein and transfers the electrons to NAD+, to form NADH . - - P37349 CPX-2634 Dha Kinase - P37349(0)|P76015(2)|P76014(2) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Catalyses the phosphorylation of dihydroxyacetone (Dha) using phosphoenolpyruvate (PEP) as a phosphoryl donor. Dihydroxyacetone phosphate (Dha-P) is an intermediate for the synthesis of pyruvate. The E1 domain of DhaM catalyses the phosphoryl transfer from PEP to the small (9 kDa) soluble HPr (histidine-containing phosphoryl carrier protein) domain. Phosphorylated DhaM binds to ADP-bound DhaL and transiently phosphorylates the ADP. ATP-loaded DhaL associates with DhaK containing the Dha substrate covalently bound to His-218 through a hemiaminal bond. Coenzyme, ATP-bound DhaL transfers a phosphate to Dha yielding Dha-P. - - P60422 CPX-1944 DnaA-L2 DnaA ribosomal protein L2 complex|DnaA-L2 complex|DnaA-rL2|DnaA-rL2 complex P03004(0)|P60422(0) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-6552976 Contributes to the regulation of replication initiation preventing multiple replication origins during one replication cycle: L2 interacts with N-terminal domain of DnaA inhibiting DnaA multimerization and therefore inhibiting further replication initiation. - DnaA is an oligomer but probably forms heterodimers with rL2. P60422 CPX-3807 50S large ribosomal subunit 50S subunit P0A7P5(1)|P0A7N1(1)|URS000002D309_83333(1)|URS00005B2216_83333(1)|P0A7Q6(1)|P02413(1)|P0A7Q1(1)|P0AG48(1)|P0AG51(1)|P0AG44(1)|P0AA10(1)|P0A7R1(1)|P0A7M2(1)|P0C018(1)|P0A7N4(1)|P0A7M6(1)|P0A7N9(1)|P0A7K6(1)|P68919(1)|P0ADY3(1)|P60438(1)|P60624(1)|P0ADY7(1)|P0ADZ0(1)|P0A7M9(1)|P0A7L3(1)|P0A7L8(1)|P0A7J7(1)|P0A7L0(1)|P0A7J3(1)|P61175(1)|P60422(1)|P60723(1)|P0AG55(1)|P0A7K2(4)|P62399(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit (CPX-3802) which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 30S subunit is responsible for the catalytic activity of the ribosome, the peptidyltransferase activity required to catalyze peptide bond formation. rplL forms dimers with an elongated shape. Two dimers associate with a copy of rplJ to form part of the L8 ribosomal stalk. The ribosomal stalk helps the ribosome interact with GTP-bound translation factors. Hetero39-mer P60438 CPX-3807 50S large ribosomal subunit 50S subunit P0A7P5(1)|P0A7N1(1)|URS000002D309_83333(1)|URS00005B2216_83333(1)|P0A7Q6(1)|P02413(1)|P0A7Q1(1)|P0AG48(1)|P0AG51(1)|P0AG44(1)|P0AA10(1)|P0A7R1(1)|P0A7M2(1)|P0C018(1)|P0A7N4(1)|P0A7M6(1)|P0A7N9(1)|P0A7K6(1)|P68919(1)|P0ADY3(1)|P60438(1)|P60624(1)|P0ADY7(1)|P0ADZ0(1)|P0A7M9(1)|P0A7L3(1)|P0A7L8(1)|P0A7J7(1)|P0A7L0(1)|P0A7J3(1)|P61175(1)|P60422(1)|P60723(1)|P0AG55(1)|P0A7K2(4)|P62399(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit (CPX-3802) which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 30S subunit is responsible for the catalytic activity of the ribosome, the peptidyltransferase activity required to catalyze peptide bond formation. rplL forms dimers with an elongated shape. Two dimers associate with a copy of rplJ to form part of the L8 ribosomal stalk. The ribosomal stalk helps the ribosome interact with GTP-bound translation factors. Hetero39-mer P60723 CPX-3807 50S large ribosomal subunit 50S subunit P0A7P5(1)|P0A7N1(1)|URS000002D309_83333(1)|URS00005B2216_83333(1)|P0A7Q6(1)|P02413(1)|P0A7Q1(1)|P0AG48(1)|P0AG51(1)|P0AG44(1)|P0AA10(1)|P0A7R1(1)|P0A7M2(1)|P0C018(1)|P0A7N4(1)|P0A7M6(1)|P0A7N9(1)|P0A7K6(1)|P68919(1)|P0ADY3(1)|P60438(1)|P60624(1)|P0ADY7(1)|P0ADZ0(1)|P0A7M9(1)|P0A7L3(1)|P0A7L8(1)|P0A7J7(1)|P0A7L0(1)|P0A7J3(1)|P61175(1)|P60422(1)|P60723(1)|P0AG55(1)|P0A7K2(4)|P62399(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit (CPX-3802) which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 30S subunit is responsible for the catalytic activity of the ribosome, the peptidyltransferase activity required to catalyze peptide bond formation. rplL forms dimers with an elongated shape. Two dimers associate with a copy of rplJ to form part of the L8 ribosomal stalk. The ribosomal stalk helps the ribosome interact with GTP-bound translation factors. Hetero39-mer P60752 CPX-2116 MsbA transporter complex Lipid A export ATP-binding/permease complex MsbA|bacterial ABC lipid flippase MsbA complex P60752(1)|P60752(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-15671289 Member of the ATP-binding cassette (ABC) transporter proteins that facilitates the export of lipid A and lipopolysaccheride across the plasma membrane. Each chain of the homodimer contains two domains, both of which dimerize: the transmembrane domains (TMD) form a pore in the plasma membrane and the cytoplasmic ATP-binding domain (NBD) is responsible for energy generation. In the active state the NBDs are open and the complex faces inwards. Upon ATP binding, the NBDs close, hydrolysis of ATP enables lipid transport through the pore of the TMDs and the complex opens up towards the periplasmic space releasing the transported lipid. The MabA dimer is also capable of transporting a wide spectrum of drugs through the plasma membrane. Homodimer with ATP binding to nucleotide binding domain (NBD). Homodimer P60752 CPX-2116 MsbA transporter complex Lipid A export ATP-binding/permease complex MsbA|bacterial ABC lipid flippase MsbA complex P60752(1)|P60752(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-15671289 Member of the ATP-binding cassette (ABC) transporter proteins that facilitates the export of lipid A and lipopolysaccheride across the plasma membrane. Each chain of the homodimer contains two domains, both of which dimerize: the transmembrane domains (TMD) form a pore in the plasma membrane and the cytoplasmic ATP-binding domain (NBD) is responsible for energy generation. In the active state the NBDs are open and the complex faces inwards. Upon ATP binding, the NBDs close, hydrolysis of ATP enables lipid transport through the pore of the TMDs and the complex opens up towards the periplasmic space releasing the transported lipid. The MabA dimer is also capable of transporting a wide spectrum of drugs through the plasma membrane. Homodimer with ATP binding to nucleotide binding domain (NBD). Homodimer P61175 CPX-3807 50S large ribosomal subunit 50S subunit P0A7P5(1)|P0A7N1(1)|URS000002D309_83333(1)|URS00005B2216_83333(1)|P0A7Q6(1)|P02413(1)|P0A7Q1(1)|P0AG48(1)|P0AG51(1)|P0AG44(1)|P0AA10(1)|P0A7R1(1)|P0A7M2(1)|P0C018(1)|P0A7N4(1)|P0A7M6(1)|P0A7N9(1)|P0A7K6(1)|P68919(1)|P0ADY3(1)|P60438(1)|P60624(1)|P0ADY7(1)|P0ADZ0(1)|P0A7M9(1)|P0A7L3(1)|P0A7L8(1)|P0A7J7(1)|P0A7L0(1)|P0A7J3(1)|P61175(1)|P60422(1)|P60723(1)|P0AG55(1)|P0A7K2(4)|P62399(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit (CPX-3802) which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 30S subunit is responsible for the catalytic activity of the ribosome, the peptidyltransferase activity required to catalyze peptide bond formation. rplL forms dimers with an elongated shape. Two dimers associate with a copy of rplJ to form part of the L8 ribosomal stalk. The ribosomal stalk helps the ribosome interact with GTP-bound translation factors. Hetero39-mer P62399 CPX-3807 50S large ribosomal subunit 50S subunit P0A7P5(1)|P0A7N1(1)|URS000002D309_83333(1)|URS00005B2216_83333(1)|P0A7Q6(1)|P02413(1)|P0A7Q1(1)|P0AG48(1)|P0AG51(1)|P0AG44(1)|P0AA10(1)|P0A7R1(1)|P0A7M2(1)|P0C018(1)|P0A7N4(1)|P0A7M6(1)|P0A7N9(1)|P0A7K6(1)|P68919(1)|P0ADY3(1)|P60438(1)|P60624(1)|P0ADY7(1)|P0ADZ0(1)|P0A7M9(1)|P0A7L3(1)|P0A7L8(1)|P0A7J7(1)|P0A7L0(1)|P0A7J3(1)|P61175(1)|P60422(1)|P60723(1)|P0AG55(1)|P0A7K2(4)|P62399(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). A ribosome is made two subunits - a smaller 30S subunit (CPX-3802) which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 30S subunit is responsible for the catalytic activity of the ribosome, the peptidyltransferase activity required to catalyze peptide bond formation. rplL forms dimers with an elongated shape. Two dimers associate with a copy of rplJ to form part of the L8 ribosomal stalk. The ribosomal stalk helps the ribosome interact with GTP-bound translation factors. Hetero39-mer P68187 CPX-1932 Maltose transport complex MalE-MalFGK2 complex|maltose transporter|maltose transporter malE-MalFGK2|maltose transporter MalE-MalFGK2 complex|maltose-transporting ATPase|maltose ATP-binding cassette (ABC) transporter complex|ATP phosphohydrolase (maltose-importing) P68187(2)|CHEBI:17306(1)|P02916(1)|P0AEX9(1)|P68183(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-6477279 Transports maltose from the periplasmic space into the cytoplasm through an ATP-dependent transmembrane channel. Maltose binds to malE which attaches to the malFG dimer. Upon release of the maltose into the transmembrane channel, the malK2 dimer binds ATP the hydrolysis of which triggers the release of maltose into the cytoplasm. Consists of periplasmic maltose binding protein MalE (P0AEX9), transmembrane MalF-MalG dimer (P02916-P68183) and cytoplasmic ATPase subunit MalK dimer (P68187). Heteropentamer P68187 CPX-1978 Enzyme IIA-maltose transporter complex maltose transporter inhibitor complex|maltose transporter repressor complex|maltose transporter MalFGK2-EIIA-Glc complex|MalFGK2-EIIA-Glc complex|EIIA(Glc)-maltose transporter complex|EIIA(Glc)–MalFGK2 complex|MalG-MalH-2xMalK-PtgA complex P69783(2)|P68187(2)|P02916(1)|P68183(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-16061739 Binding of enzyme IIA (EIIA-Glc), a component of the glucose-specific phosphotransferase system, inhibits maltose transport from the periplasm to the cytoplasm. Two molecules of EIIA-Glc each bind allosterically to both subunits of MalK thereby fastening the maltose transporter in the open, inward-facing conformation which prevents the binding of maltose-loaded maltose binding protein MBP (MalE) (CPX-1932). Only the non-phosphorylated form of enzyme IIA functions as a maltose uptake inhibitor. - Heterohexamer P68187 CPX-2103 MalFGK2 maltose transport complex maltose transport MalFGK2 complex|maltose transport complex, core subunit P02916(1)|P68187(2)|P68183(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-6477279 Central subunit of the maltose transporter (CPX-1932). Maltose transport is initiated when maltose-bound maltose binding protein MalE (P0AEX9) binds to this subunit on the periplasmic site of the plasma membrane. Heterotetramer, consist of MalK homodimer and MalF and MalG monomers. Heterotetramer P69222 CPX-2244 Translation initiation factor complex 30S ribosomal translation pre-initiation complex P0A707(0)|P0A705(1)|P69222(1) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Required for initiation of protein synthesis, when the ribosome recruits an mRNA for translation and establishes the reading frame by binding initiator tRNA to the start codon in the P site of the small (30S) ribosomal subunit (CPX-3802). Assembles on the 30S subunit to form a transient 30S preinitiation complex (PIC). IF3 and IF2 are the first factors to arrive, forming an unstable 30S–IF2–IF3 complex. Subsequently, IF1 joins and locks the factors in a kinetically stable 30S PIC to which fMet-tRNAfMet is recruited. The complex dissociates on binding of the 50S ribosomal subunit. - - P69428 CPX-3445 Twin-arginine translocation complex TAT complex P0A843(0)|P69423(0)|P69428(0)|P69425(0) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Proton motive force dependent transporter of folded precursor proteins containing a SRRxFLK (TAT) sequence motif in the N-terminal part of their signal sequences across the cytoplasmic membrane. tatB binds to two different sites on tatC monomers thereby forming circular, hetero-multimeric substrate receptor complexes. tatA associates with tatB-tatC and the signal peptide and may oligmerise to form the translocation pore. tatE could fulfil a role in the recruitment of tatA to the tatBC receptor complex through hetero-oligomerization with tatA and may function as a nucleation point for tatBC-dependent oligomerization of tatA. - P69783 CPX-1978 Enzyme IIA-maltose transporter complex maltose transporter inhibitor complex|maltose transporter repressor complex|maltose transporter MalFGK2-EIIA-Glc complex|MalFGK2-EIIA-Glc complex|EIIA(Glc)-maltose transporter complex|EIIA(Glc)–MalFGK2 complex|MalG-MalH-2xMalK-PtgA complex P69783(2)|P68187(2)|P02916(1)|P68183(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-16061739 Binding of enzyme IIA (EIIA-Glc), a component of the glucose-specific phosphotransferase system, inhibits maltose transport from the periplasm to the cytoplasm. Two molecules of EIIA-Glc each bind allosterically to both subunits of MalK thereby fastening the maltose transporter in the open, inward-facing conformation which prevents the binding of maltose-loaded maltose binding protein MBP (MalE) (CPX-1932). Only the non-phosphorylated form of enzyme IIA functions as a maltose uptake inhibitor. - Heterohexamer P76014 CPX-2634 Dha Kinase - P37349(0)|P76015(2)|P76014(2) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Catalyses the phosphorylation of dihydroxyacetone (Dha) using phosphoenolpyruvate (PEP) as a phosphoryl donor. Dihydroxyacetone phosphate (Dha-P) is an intermediate for the synthesis of pyruvate. The E1 domain of DhaM catalyses the phosphoryl transfer from PEP to the small (9 kDa) soluble HPr (histidine-containing phosphoryl carrier protein) domain. Phosphorylated DhaM binds to ADP-bound DhaL and transiently phosphorylates the ADP. ATP-loaded DhaL associates with DhaK containing the Dha substrate covalently bound to His-218 through a hemiaminal bond. Coenzyme, ATP-bound DhaL transfers a phosphate to Dha yielding Dha-P. - - P76015 CPX-2634 Dha Kinase - P37349(0)|P76015(2)|P76014(2) ECO:0005547(biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion) - Catalyses the phosphorylation of dihydroxyacetone (Dha) using phosphoenolpyruvate (PEP) as a phosphoryl donor. Dihydroxyacetone phosphate (Dha-P) is an intermediate for the synthesis of pyruvate. The E1 domain of DhaM catalyses the phosphoryl transfer from PEP to the small (9 kDa) soluble HPr (histidine-containing phosphoryl carrier protein) domain. Phosphorylated DhaM binds to ADP-bound DhaL and transiently phosphorylates the ADP. ATP-loaded DhaL associates with DhaK containing the Dha substrate covalently bound to His-218 through a hemiaminal bond. Coenzyme, ATP-bound DhaL transfers a phosphate to Dha yielding Dha-P. - - P76194 CPX-2125 SufE complex sulfur acceptor protein complex SufE P76194(2) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-8793970 Sulfur transfer homodimer that accepts the atomic sulfur resulting from the L-cysteine desulfurase activity of SufS (CPX-2124 [SufS dimer], EBI-8843399 [transfer interaction]) and further transfers it to the SufBCD scaffold protein complex (CPX-2123 [complex], EBI-8844754 [transfer interaction]). It is a component of the sufABCDSE operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. It plays a role in the iron-sulfur cluster formation on SufBCD. Homodimer Homodimer P76398 CPX-2119 MdtBC complex MdtBC efflux pump|MdtBC multidrug efflux pump P76398(2)|P76399(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-6515216 Involved in the resistance of gram negative bacteria to novobiocin, deoxycholate and beta-lactams. MdtB and MdtC are transmembrane proteins facilitating drug export while MdtA is the (cytoplasmic?) membrane fusion protein associated with MdtBC (no binding data available yet). MdtABC requires TolC (P02930), an outer membrane 'channel-tunnel' trimer, for its function. The composition of the of the MdtABC holo-transporter maybe variably composted of the MdtA, MdtB and MdtC subunits, however, either MdtB or MdtC must the present. The mdtABC operon is transcriptionally activated by BaeR (P69228). Heterotrimer, consisting of two MdtB and one MdtC subunits. Heterotrimer P77522 CPX-2123 SufBCD complex SufB-SufC-SufD complex|SufBCD tetramer P77522(1)|P77499(2)|P77689(1) ECO:0000353(physical interaction evidence used in manual assertion) intact:EBI-8845643 Scaffold complex that assembles an Fe-S cluster. The SufB protomer of the SufBCD complex accepts the atomic sulfur from the sulfur transfer protein SufE (CPX-2125 [SufE dimer], EBI-8844754 [transfer interaction]) and incorporates it into an [4Fe-4S] cluster in an as yet undiscovered manner. SufBCD further transfers the Fe-S cluster to the carrier protein SufA (CPX-2142 [dimer], EBI-8805910 [transfer interaction]). SufBCD is a component of the sufABCDSE operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. The SufBCD complex is a putative ATP-binding cassette (ABC) transporter complex, inferred by its structural similarity with other ABC transporters. SufC has been shown to be an ATPase whose activity is enhanced by the presence of SufB and SufD (PMID:20857974). The precise function of FADH2 is not yet clear. Under aerobic conditions FADH2 is oxidised to FAD and dissociates from SufBCD. Probable heteroteramer, consisting of two SufC subunits and one SufB and SufD subunit each and a FADH2 cofactor. MW = 160 kD In vitro, the following alternative conformations (incl stoichiometry) were found: SufB2C2 (possibly in vivo conformation), SufC2D2 and SufB1C1D1. Heterotetramer