Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Acetyladenylate or its derivative acetylates the chemotaxis protein CheY in vitro and increases its activity at the flagellar switch.
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Producing acetyladenylate inside cytoplasm-free bacterial envelopes containing purified CheY, Acs and ATP acetylated CheY on nitrogen and raised the fraction of clockwise-rotating envelopes from 14% to 58%.
"Acetylated CheY was stable in the presence of the strong nucleophiles hydroxylamine or ethanolamine, indicative of N-acetylation"
Acetylation of the response regulator, CheY, is involved in bacterial chemotaxis.
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An acs deletion mutant showed much reduced sensitivity to both attractants and repellents in tethering assays and reduced responses in ring-forming, plug and capillary assays.
"The Deltaacs mutant exhibited much reduced sensitivity to chemotactic stimuli (both attractants and repellents) in tethering assays and greatly reduced responses in ring-forming, plug and capillary assays."
Structure and substrate binding properties of cobB, a Sir2 homolog protein deacetylase from Escherichia coli.
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CobB is a bacterial sirtuin that deacetylates Acs at an active-site lysine and thereby stimulates Acs activity; calorimetry with intact acetylated Acs indicates recognition beyond the acetyl-lysine site.
"cobB is a bacterial sirtuin that deacetylates acetyl-CoA synthetase (Acs) at an active site lysine to stimulate its enzymatic activity"
Identification of the protein acetyltransferase (Pat) enzyme that acetylates acetyl-CoA synthetase in Salmonella enterica.
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Pat, a GNAT acetyltransferase, is the major protein acetyltransferase of Salmonella enterica and uses acetyl-CoA to acetylate Acs residue Lys609, which together with the CobB sirtuin regulates Acs activity.
"The Pat enzyme uses acetyl-CoA as substrate to modify residue Lys609 of Acs"
Acetylation of the chemotaxis response regulator CheY by acetyl-CoA synthetase purified from Escherichia coli.
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Acs overproduced and purified from E. coli behaved as a typical prokaryotic Acs enzyme, with Mg(2+) as the preferred cofactor; this is the characterization EcoCyc used for both the acetyl-CoA synthetase and the propionate-CoA ligase IDA rows.
"The enzyme exhibited characteristics typical of prokaryotic Acs enzymes"
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Purified Acs acetylated CheY using either acetate or acetyl-CoA as the acetyl donor, and the reaction was reversible and cooperative with a Hill coefficient of about 3.
"it could use either acetate or AcCoA as an acetyl donor for CheY acetylation. The Acs-catalyzed acetylation of CheY was reversible, an essential property for a regulatory process, and cooperative (Hill coefficient approximately 3)"
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Mass spectrometry of tryptic digests mapped CheY acetylation to C-terminal lysines 91, 92, 109, 119, 122 and 126, and Acs itself was shown to autoacetylate.
"the acetylation sites of CheY are clustered at the C terminus of the protein, with lysine residues 91, 92, 109, 119, 122 and 126 being the main acetylation sites"
The chemotaxis response regulator CheY can catalyze its own acetylation.
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CheY purified from an acs deletion mutant was still partially acetylated, and [14C]acetyl-CoA labelling in the absence of Acs showed that CheY autoacetylates at a rate similar to Acs-mediated acetylation.
"this protein is partially acetylated in spite of the absence of Acs, suggesting that CheY can be post-translationally acetylated in vivo by additional means"
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Autoacetylated CheY, like Acs-acetylated CheY, could be deacetylated by Acs, which is the reverse direction of the Acs acetyl-transfer reaction rather than a hydrolytic deacetylation.
"Like CheY acetylated by Acs, autoacetylated CheY could be deacetylated by Acs"
Protein abundance profiling of the Escherichia coli cytosol.
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LC-MS/MS with protein and peptide fractionation identified 1103 proteins from the cytosolic fraction of E. coli MC4100 with emPAI abundance estimates; Acs appears in the supplementary abundance table rather than in the article body.
"we identified 1103 proteins from the cytosolic fraction of the Escherichia coli strain MC4100"
CobB regulates Escherichia coli chemotaxis by deacetylating the response regulator CheY.
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CobB deacetylates both Acs and CheY in vitro, and a cobB deletion is chemotaxis-impaired while an acs deletion is not, in two independent strain backgrounds.
"In contrast, the Δacs mutant was indistinguishable from the W3110 parental strain (Fig. 4B). To confirm that the similarity between them was not strain dependent, strains AJW613 and its Δacs mutant derivative AJW803 were also examined and similar results were observed"
The enzymic interconversion of acetate and acetyl-coenzyme A in Escherichia coli.
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An inducible acetyl-CoA synthetase (acetate--CoA ligase, AMP-forming; EC 6.2.1.1) effects acetate uptake in E. coli mutants lacking acetate kinase or phosphotransacetylase, establishing the activity physiologically before the gene was cloned.
"An inducible acetyl-CoA synthetase [acetate: CoA ligase (AMP-forming); EC 6.2.1.1] effects this uptake of acetate"
Acetyl-phosphate is a critical determinant of lysine acetylation in E. coli.
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Most E. coli lysine acetylation occurs at low stoichiometry, accumulates in growth-arrested cells, depends on acetyl-phosphate formation, and acetyl-phosphate acetylates lysines chemically in vitro, so acetylation levels can reflect acyl-donor supply rather than acetyltransferase activity.
"We showed that AcP can chemically acetylate lysine residues in vitro and that AcP levels are correlated with acetylation levels in vivo, suggesting that AcP may acetylate proteins nonenzymatically in cells"
Acs is essential for propionate utilization in Escherichia coli.
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Reversible acetylation modulates the propionyl-CoA synthetase activity of Acs, and deleting acs blocks propionate utilization in E. coli, while deleting cobB impairs growth only at lower propionate concentrations.
"Results from biochemical analysis showed that, reversible acetylation also modulates the propionyl-CoA synthetase activity of Acs. Subsequent genetic analysis revealed that, deletion of acs in E. coli results in blockage of propionate utilization"
Structural basis of the catalytic and allosteric mechanism of bacterial acetyltransferase PatZ.
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PatZ, the E. coli Type I GNAT protein acetyltransferase, is a homotetramer whose regulatory domain is required for acetyltransferase activity, and its substrates include Acs Lys609.
"Our results demonstrate that the regulatory domain is vital for acetyltransferase activity, as it triggers cooperative conformational changes in the catalytic domain and directly aids in the formation of substrate-binding pockets."
Cloning, characterization, and functional expression of acs, the gene which encodes acetyl coenzyme A synthetase in Escherichia coli.
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The subcloned ORF encodes a 72-kDa protein that, when purified in the presence of coenzyme A, activates acetate in a CoA-dependent manner; anti-Acs antiserum detects the band in wild type but not in the acs deletion.
"When purified in the presence, but not in the absence, of coenzyme A, the E. coli enzyme activated acetate across a wide range of concentrations in a coenzyme A-dependent manner. On the basis of these and other observations, we conclude that this open reading frame encodes the acetate-activating enzyme, Acs."
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Cells deleted for acs grow poorly on low acetate (at or below 10 mM) while ackA pta deletions grow poorly on high acetate, and the triple deletion cannot grow on acetate at any concentration; plasmid-borne acs restores growth to the triple mutant.
"those deleted for acs grew poorly on low concentrations (< or = 10 mM), those deleted for ackA and pta (which encode Ack and Pta, respectively) grew poorly on high concentrations (> or = 25 mM), and those deleted for acs, ackA, and pta did not grow on acetate at any concentration tested"
UniProtKB P27550 (ACSA_ECOLI) curated record
acs curation notes (literature synthesis; deep research unavailable in this environment)