acetyl-CoA synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.

Chemotaxis regulator transmitting signal to flagellar motor component; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. In its active (phosphorylated or acetylated) form, CheY exhibits enhanced binding to a switch component, FliM, at the flagellar motor which induces a change from counterclockwise to clockwise flagellar rotation. Overexpression of CheY in association with MotA and MotB improves motility of a ycgR disruption, suggesting there is an interaction (direct or indirect) between the c-di-GMP-binding flagellar brake protein and th [...]

acetyl-CoA synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.

Deacetylase of acs and cheY, chemotaxis regulator; NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. Activates the enzyme acetyl-CoA synthetase by deacetylating 'Lys-609' in the inactive, acetylated form of the enzyme. May also modulate the activity of other propionyl-adenosine monophosphate (AMP)-forming enzymes. Belongs to the sirtuin family. Class III subfamily.

acetyl-CoA synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.

Protein lysine acetyltransferase; Catalyzes the acetyl-CoA-dependent acetylation of lysine residues of a large number of target proteins. Acetylates RNase R in exponential phase cells and RNase II. Required for the glucose-dependent acetylation on multiple lysines of alpha, beta and beta' RNAP subunits. Also acetylates acetyl-coenzyme A synthetase (Acs) and the chromosomal replication initiator protein DnaA, and inhibits their activity. Overexpression leads to the acetylation of a large number of additional proteins and inhibits motility.

Chemotaxis regulator transmitting signal to flagellar motor component; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. In its active (phosphorylated or acetylated) form, CheY exhibits enhanced binding to a switch component, FliM, at the flagellar motor which induces a change from counterclockwise to clockwise flagellar rotation. Overexpression of CheY in association with MotA and MotB improves motility of a ycgR disruption, suggesting there is an interaction (direct or indirect) between the c-di-GMP-binding flagellar brake protein and th [...]

acetyl-CoA synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.

Chemotaxis regulator transmitting signal to flagellar motor component; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. In its active (phosphorylated or acetylated) form, CheY exhibits enhanced binding to a switch component, FliM, at the flagellar motor which induces a change from counterclockwise to clockwise flagellar rotation. Overexpression of CheY in association with MotA and MotB improves motility of a ycgR disruption, suggesting there is an interaction (direct or indirect) between the c-di-GMP-binding flagellar brake protein and th [...]

N-hydroxyarylamine O-acetyltransferase; Catalyzes the acetyl-CoA-dependent N-acetylation of aromatic amines, and, probably, the O-acetylation of N-hydroxyarylamines. In vitro, catalyzes the N-acetylation of various arylamines such as aminobenzoic acid, aminophenol, aminotoluene, phenetidine, anisidine, aniline, isoniazid and 2-amino-fluorene. N-hydroxyarylamine O-acetyltransferase activity has not been assayed directly, however, NhoA activity is required for the mutagenicity of nitroaromatic compounds, suggesting that it also has O- acetyltransferase activity (Probable).

Chemotaxis regulator transmitting signal to flagellar motor component; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. In its active (phosphorylated or acetylated) form, CheY exhibits enhanced binding to a switch component, FliM, at the flagellar motor which induces a change from counterclockwise to clockwise flagellar rotation. Overexpression of CheY in association with MotA and MotB improves motility of a ycgR disruption, suggesting there is an interaction (direct or indirect) between the c-di-GMP-binding flagellar brake protein and th [...]

Protein lysine acetyltransferase; Catalyzes the acetyl-CoA-dependent acetylation of lysine residues of a large number of target proteins. Acetylates RNase R in exponential phase cells and RNase II. Required for the glucose-dependent acetylation on multiple lysines of alpha, beta and beta' RNAP subunits. Also acetylates acetyl-coenzyme A synthetase (Acs) and the chromosomal replication initiator protein DnaA, and inhibits their activity. Overexpression leads to the acetylation of a large number of additional proteins and inhibits motility.

Chemotaxis regulator transmitting signal to flagellar motor component; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. In its active (phosphorylated or acetylated) form, CheY exhibits enhanced binding to a switch component, FliM, at the flagellar motor which induces a change from counterclockwise to clockwise flagellar rotation. Overexpression of CheY in association with MotA and MotB improves motility of a ycgR disruption, suggesting there is an interaction (direct or indirect) between the c-di-GMP-binding flagellar brake protein and th [...]

Response regulator in two-component regulatory system with RcsC and YojN; Component of the Rcs signaling system, which controls transcription of numerous genes. RcsB is the response regulator that binds to regulatory DNA regions. Can function both in an RcsA-dependent or RcsA-independent manner. The system regulates expression of numerous genes, including genes involved in colanic acid capsule synthesis, biofilm formation, cell division and outer membrane proteins synthesis. Also involved, with GadE, in control of glutamate-dependent acid resistance, and, with BglJ, in derepression of [...]

Deacetylase of acs and cheY, chemotaxis regulator; NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. Activates the enzyme acetyl-CoA synthetase by deacetylating 'Lys-609' in the inactive, acetylated form of the enzyme. May also modulate the activity of other propionyl-adenosine monophosphate (AMP)-forming enzymes. Belongs to the sirtuin family. Class III subfamily.

acetyl-CoA synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.

Deacetylase of acs and cheY, chemotaxis regulator; NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. Activates the enzyme acetyl-CoA synthetase by deacetylating 'Lys-609' in the inactive, acetylated form of the enzyme. May also modulate the activity of other propionyl-adenosine monophosphate (AMP)-forming enzymes. Belongs to the sirtuin family. Class III subfamily.

Putative dihydroxyacetone-specific PTS enzymes: HPr, EI components; Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine residues finally leads to phosphoryl transfer to DhaL and dihydroxyacetone.

Deacetylase of acs and cheY, chemotaxis regulator; NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. Activates the enzyme acetyl-CoA synthetase by deacetylating 'Lys-609' in the inactive, acetylated form of the enzyme. May also modulate the activity of other propionyl-adenosine monophosphate (AMP)-forming enzymes. Belongs to the sirtuin family. Class III subfamily.

Methionine N-acyltransferase; Acyltransferase that appears to be required for E.coli optimal growth rate and yield via the formation of N-acetylated amino acids. Catalyzes the acylation of L-methionine using acetyl-CoA or propanoyl-CoA as acyl donors, and the acetylation of L-phenylglycine. Is also able to N-acylate other free L-amino acids and their derivatives using a CoA thioester as cosubstrate. Using acetyl-CoA as an acyl donor, substrate specificity is methionine sulfone > methionine sulfoximine > methionine sulfoxide > methionine. Asparagine, lysine, glutamine, aspartate and glu [...]

Deacetylase of acs and cheY, chemotaxis regulator; NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. Activates the enzyme acetyl-CoA synthetase by deacetylating 'Lys-609' in the inactive, acetylated form of the enzyme. May also modulate the activity of other propionyl-adenosine monophosphate (AMP)-forming enzymes. Belongs to the sirtuin family. Class III subfamily.

N-hydroxyarylamine O-acetyltransferase; Catalyzes the acetyl-CoA-dependent N-acetylation of aromatic amines, and, probably, the O-acetylation of N-hydroxyarylamines. In vitro, catalyzes the N-acetylation of various arylamines such as aminobenzoic acid, aminophenol, aminotoluene, phenetidine, anisidine, aniline, isoniazid and 2-amino-fluorene. N-hydroxyarylamine O-acetyltransferase activity has not been assayed directly, however, NhoA activity is required for the mutagenicity of nitroaromatic compounds, suggesting that it also has O- acetyltransferase activity (Probable).

Deacetylase of acs and cheY, chemotaxis regulator; NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. Activates the enzyme acetyl-CoA synthetase by deacetylating 'Lys-609' in the inactive, acetylated form of the enzyme. May also modulate the activity of other propionyl-adenosine monophosphate (AMP)-forming enzymes. Belongs to the sirtuin family. Class III subfamily.

Protein lysine acetyltransferase; Catalyzes the acetyl-CoA-dependent acetylation of lysine residues of a large number of target proteins. Acetylates RNase R in exponential phase cells and RNase II. Required for the glucose-dependent acetylation on multiple lysines of alpha, beta and beta' RNAP subunits. Also acetylates acetyl-coenzyme A synthetase (Acs) and the chromosomal replication initiator protein DnaA, and inhibits their activity. Overexpression leads to the acetylation of a large number of additional proteins and inhibits motility.

Deacetylase of acs and cheY, chemotaxis regulator; NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. Activates the enzyme acetyl-CoA synthetase by deacetylating 'Lys-609' in the inactive, acetylated form of the enzyme. May also modulate the activity of other propionyl-adenosine monophosphate (AMP)-forming enzymes. Belongs to the sirtuin family. Class III subfamily.

Response regulator in two-component regulatory system with RcsC and YojN; Component of the Rcs signaling system, which controls transcription of numerous genes. RcsB is the response regulator that binds to regulatory DNA regions. Can function both in an RcsA-dependent or RcsA-independent manner. The system regulates expression of numerous genes, including genes involved in colanic acid capsule synthesis, biofilm formation, cell division and outer membrane proteins synthesis. Also involved, with GadE, in control of glutamate-dependent acid resistance, and, with BglJ, in derepression of [...]

Deacetylase of acs and cheY, chemotaxis regulator; NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. Activates the enzyme acetyl-CoA synthetase by deacetylating 'Lys-609' in the inactive, acetylated form of the enzyme. May also modulate the activity of other propionyl-adenosine monophosphate (AMP)-forming enzymes. Belongs to the sirtuin family. Class III subfamily.

GNAT family putative N-acetyltransferase; N-epsilon-lysine acetyltransferase that catalyzes acetylation of a large number of proteins. Overexpression inhibits motility.

Deacetylase of acs and cheY, chemotaxis regulator; NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. Activates the enzyme acetyl-CoA synthetase by deacetylating 'Lys-609' in the inactive, acetylated form of the enzyme. May also modulate the activity of other propionyl-adenosine monophosphate (AMP)-forming enzymes. Belongs to the sirtuin family. Class III subfamily.

GNAT-family putative N-acetyltransferase; N-epsilon-lysine acetyltransferase that catalyzes acetylation of a large number of proteins. Binds acetyl-CoA ; Belongs to the acetyltransferase family.

Putative dihydroxyacetone-specific PTS enzymes: HPr, EI components; Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine residues finally leads to phosphoryl transfer to DhaL and dihydroxyacetone.

Deacetylase of acs and cheY, chemotaxis regulator; NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. Activates the enzyme acetyl-CoA synthetase by deacetylating 'Lys-609' in the inactive, acetylated form of the enzyme. May also modulate the activity of other propionyl-adenosine monophosphate (AMP)-forming enzymes. Belongs to the sirtuin family. Class III subfamily.

Putative dihydroxyacetone-specific PTS enzymes: HPr, EI components; Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine residues finally leads to phosphoryl transfer to DhaL and dihydroxyacetone.

N-hydroxyarylamine O-acetyltransferase; Catalyzes the acetyl-CoA-dependent N-acetylation of aromatic amines, and, probably, the O-acetylation of N-hydroxyarylamines. In vitro, catalyzes the N-acetylation of various arylamines such as aminobenzoic acid, aminophenol, aminotoluene, phenetidine, anisidine, aniline, isoniazid and 2-amino-fluorene. N-hydroxyarylamine O-acetyltransferase activity has not been assayed directly, however, NhoA activity is required for the mutagenicity of nitroaromatic compounds, suggesting that it also has O- acetyltransferase activity (Probable).

Putative dihydroxyacetone-specific PTS enzymes: HPr, EI components; Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine residues finally leads to phosphoryl transfer to DhaL and dihydroxyacetone.

Protein lysine acetyltransferase; Catalyzes the acetyl-CoA-dependent acetylation of lysine residues of a large number of target proteins. Acetylates RNase R in exponential phase cells and RNase II. Required for the glucose-dependent acetylation on multiple lysines of alpha, beta and beta' RNAP subunits. Also acetylates acetyl-coenzyme A synthetase (Acs) and the chromosomal replication initiator protein DnaA, and inhibits their activity. Overexpression leads to the acetylation of a large number of additional proteins and inhibits motility.

GNAT family putative N-acetyltransferase; Belongs to the UPF0039 (ElaA) family.

Methionine N-acyltransferase; Acyltransferase that appears to be required for E.coli optimal growth rate and yield via the formation of N-acetylated amino acids. Catalyzes the acylation of L-methionine using acetyl-CoA or propanoyl-CoA as acyl donors, and the acetylation of L-phenylglycine. Is also able to N-acylate other free L-amino acids and their derivatives using a CoA thioester as cosubstrate. Using acetyl-CoA as an acyl donor, substrate specificity is methionine sulfone > methionine sulfoximine > methionine sulfoxide > methionine. Asparagine, lysine, glutamine, aspartate and glu [...]

GNAT family putative N-acetyltransferase; Belongs to the UPF0039 (ElaA) family.

PanD autocleavage accelerator, panothenate synthesis; Controls both the activation and catalytic activity of PanD in a coenzyme A (CoA)-dependent fashion. Binding of CoA or a derivative to PanZ leads to interaction with PanD, which promotes the processing and activation of pro-PanD, and subsequent substrate-mediated inhibition of the active form of PanD. Inhibition of PanD activity is probably the primary metabolic role of PanZ, allowing negative feedback regulation of pantothenate biosynthesis by CoA. Belongs to the PanZ/PanM family.