STRINGSTRING
dhaM dhaM cobB cobB yafP yafP rimJ rimJ rcsB rcsB elaA elaA ypeA ypeA tmcA tmcA pka pka yhbS yhbS yhhY yhhY panM panM yiaC yiaC wecD wecD yiiD yiiD yjaB yjaB acs acs phnO phnO yjdJ yjdJ rnr rnr yjgM yjgM yjhQ yjhQ rimI rimI yedL yedL cheY cheY speG speG nhoA nhoA mnaT mnaT
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
dhaMPutative 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. (472 aa)
cobBDeacetylase 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. (242 aa)
yafPGNAT family putative N-acetyltransferase. (150 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)
rcsBResponse 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 [...] (216 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)
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)
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)
yiaCGNAT family putative N-acetyltransferase; N-epsilon-lysine acetyltransferase that catalyzes acetylation of a large number of proteins. Overexpression inhibits motility. (146 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)
yiiDGNAT family putative N-acetyltransferase; Putative acetyltransferase. (329 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)
acsacetyl-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. (652 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)
yjdJGNAT family putative N-acetyltransferase. (90 aa)
rnrExoribonuclease R, RNase R; 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs (rRNAs, tRNAs and SsrA/tmRNA). In stationary phase, involved in the post- transcriptional regulation of ompA mRNA stability. Shortens RNA processively to di- and trinucleotides. In vitro, exhibits helicase activity, which is independent of its RNase activity. RNases 2 and R (rnb and this entry) contribute to rRNA degradation during starvation, while RNase R and PNPase (this entry and pnp) are the major contributors to quality control of rRNA duri [...] (813 aa)
yjgMGNAT family putative N-acetyltransferase; Putative acyltransferase; Belongs to the acetyltransferase family. (167 aa)
yjhQGNAT family putative N-acetyltransferase; Protein involved in RNA metabolic process; Belongs to the acetyltransferase family. (181 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)
yedLGNAT family putative N-acetyltransferase; Belongs to the acetyltransferase family. (159 aa)
cheYChemotaxis 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 [...] (129 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)
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)
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)
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
Server load: low (36%) [HD]