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yhbS yhbS yhhY yhhY yjhQ yjhQ yjgM yjgM yjdJ yjdJ phnO phnO yjaB yjaB yiiD yiiD wecD wecD rimI rimI glmU glmU yiaC yiaC panM panM yafP yafP citC citC rimJ rimJ rimL rimL mnaT mnaT nhoA nhoA speG speG yedL yedL elaA elaA ypeA ypeA tmcA tmcA pka pka argA argA
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
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Your Input:
yhbSGNAT family putative N-acetyltransferase; Belongs to the acetyltransferase family. (167 aa)
yhhYAminoacyl nucleotide detoxifying acetyltransferase; Catalyzes the N-acetylation of L-phenylalanine and L- methionine using acetyl-CoA as acetyl donor in vitro. Cannot accept L- tyrosine as substrate and propionyl-CoA, succinyl-CoA or (S)- methylmalonyl-CoA as acyl donors. Is also able to acetylate and thus detoxify several nonhydrolyzable aminoacyl adenylates, but not the processed form of the peptide-nucleotide antibiotic microcin C (McC). When overproduced, provides complete resistance to leucyl sulfamoyl adenylate (LSA) and partial resistance to alanyl sulfamoyl adenylate (ASA) and [...] (162 aa)
yjhQGNAT family putative N-acetyltransferase; Protein involved in RNA metabolic process; Belongs to the acetyltransferase family. (181 aa)
yjgMGNAT family putative N-acetyltransferase; Putative acyltransferase; Belongs to the acetyltransferase family. (167 aa)
yjdJGNAT family putative N-acetyltransferase. (90 aa)
phnOAminoalkylphosphonate N-acetyltransferase; Aminoalkylphosphonate N-acetyltransferase which is able to acetylate a range of aminoalkylphosphonic acids, including aminomethylphosphonate, (S)-1-aminoethylphosphonate and 2- aminoethyl- and 3-aminopropylphosphonate, using acetyl-CoA as acetyl donor. Is required for the utilization of aminomethylphosphonate and (S)-1-aminoethylphosphonate as a phosphate source via the C-P lyase pathway. Is also essential for the detoxification of (S)-1- aminoethylphosphonate, a structural analog of D-alanine that has bacteriocidal properties due to inhibitio [...] (144 aa)
yjaBGNAT-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. (147 aa)
yiiDGNAT family putative N-acetyltransferase; Putative acetyltransferase. (329 aa)
wecDTDP-fucosamine acetyltransferase; Catalyzes the acetylation of dTDP-fucosamine (dTDP-4-amino- 4,6-dideoxy-D-galactose) to dTDP-Fuc4NAc, which is utilized in the biosynthesis of the enterobacterial common antigen (ECA). Belongs to the WecD family. (224 aa)
rimIribosomal-protein-S18-alanine N-acetyltransferase; Acetylates the N-terminal alanine of ribosomal protein S18. Also acts as a N-epsilon-lysine acetyltransferase that catalyzes acetylation of several proteins. (148 aa)
glmUFused N-acetyl glucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyl transferase; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain. (456 aa)
yiaCGNAT family putative N-acetyltransferase; N-epsilon-lysine acetyltransferase that catalyzes acetylation of a large number of proteins. Overexpression inhibits motility. (146 aa)
panMPanD 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. (127 aa)
yafPGNAT family putative N-acetyltransferase. (150 aa)
citCCitrate lyase ligase; Acetylation of prosthetic group (2-(5''-phosphoribosyl)-3'- dephosphocoenzyme-A) of the gamma subunit of citrate lyase. (352 aa)
rimJribosomal-protein-S5-alanine N-acetyltransferase; Acetylates the N-terminal alanine of ribosomal protein S5. Also plays a role in maturation of the 30S ribosomal subunit. Plays a role in the temperature regulation of pap pilin transcription. Belongs to the acetyltransferase family. RimJ subfamily. (194 aa)
rimLribosomal-protein-L7/L12-serine acetyltransferase; This enzyme acetylates the N-terminal serine of ribosomal protein L7/L12. (179 aa)
mnaTMethionine 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 [...] (172 aa)
nhoAN-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). (281 aa)
speGSpermidine N(1)-acetyltransferase; Involved in the protection against polyamine toxicity by regulating their concentration. Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to the primary amino groups of spermidine to yield N(1)- and N(8)-acetylspermidine. It can also use polyamines such as spermine, but not putrescine. (186 aa)
yedLGNAT family putative N-acetyltransferase; Belongs to the acetyltransferase family. (159 aa)
elaAGNAT family putative N-acetyltransferase; Belongs to the UPF0039 (ElaA) family. (153 aa)
ypeAGNAT family putative N-acetyltransferase; Belongs to the acetyltransferase family. YpeA subfamily. (141 aa)
tmcAElongator methionine tRNA (ac4C34) acetyltransferase; Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP). It recognizes the wobble base of tRNA(Met), thus distinguishing between tRNA(Met) and the structurally similar tRNA(Ile2). (671 aa)
pkaProtein 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. (886 aa)
argAAmino acid N-acetyltransferase and inactive acetylglutamate kinase; N-acetylglutamate synthase; amino acid acetyltransferase; Protein involved in arginine biosynthetic process; Belongs to the acetyltransferase family. ArgA subfamily. (443 aa)
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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