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gadW gadW gadX gadX gadA gadA yhjA yhjA eptB eptB yicR yicR gyrB gyrB mdh mdh fimB fimB fimA fimA trmI trmI recA recA yfjY yfjY yfaL yfaL yeeS yeeS flu flu fumC fumC ompW ompW hlyE hlyE sfmA sfmA hha hha ykfG ykfG btuB btuB dctR dctR yhiD yhiD hdeD hdeD gadE gadE
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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.
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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
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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:
gadWTranscriptional activator of gadA and gadBC; Depending on the conditions (growth phase and medium), acts as a positive or negative regulator of gadA and gadBC. Repression occurs directly or via the repression of the expression of gadX. Activation occurs directly by the binding of GadW to the gadA and gadBC promoters. (242 aa)
gadXAcid resistance regulon transcriptional activator; Positively regulates the expression of about fifteen genes involved in acid resistance such as gadA, gadB and gadC. Depending on the conditions (growth phase and medium), can repress gadW. (274 aa)
gadAGlutamate decarboxylase A, PLP-dependent; Converts glutamate to gamma-aminobutyrate (GABA), consuming one intracellular proton in the reaction. The gad system helps to maintain a near-neutral intracellular pH when cells are exposed to extremely acidic conditions. The ability to survive transit through the acidic conditions of the stomach is essential for successful colonization of the mammalian host by commensal and pathogenic bacteria. (466 aa)
yhjAProtein involved in cytochrome complex assembly. (465 aa)
eptBKDO phosphoethanolamine transferase, Ca(2+)-inducible; Catalyzes the addition of a phosphoethanolamine (pEtN) moiety to the outer 3-deoxy-D-manno-octulosonic acid (Kdo) residue of a Kdo(2)-lipid A. Phosphatidylethanolamines with one unsaturated acyl group functions as pEtN donors and the reaction releases diacylglycerol; Belongs to the phosphoethanolamine transferase family. EptB subfamily. (563 aa)
yicRUPF0758 family protein; DNA repair protein; Protein involved in DNA-dependent DNA replication and DNA repair; Belongs to the UPF0758 family. YicR subfamily. (222 aa)
gyrBDNA gyrase, subunit B; DNA gyrase negatively supercoils closed circular double- stranded DNA in an ATP-dependent manner to maintain chromosomes in an underwound state. This makes better substrates for topoisomerase 4 (ParC and ParE) which is the main enzyme that unlinks newly replicated chromosomes in E.coli. Gyrase catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes. Relaxes negatively supercoiled DNA in an ATP-independent manner. E.coli gyrase has higher supercoiling activity than other characterized bacterial gyrases; at compa [...] (804 aa)
mdhMalate dehydrogenase, NAD(P)-binding; Catalyzes the reversible oxidation of malate to oxaloacetate. (312 aa)
fimBTyrosine recombinase/inversion of on/off regulator of fimA; FimB is one of the 2 regulatory proteins which control the phase variation of type 1 fimbriae in E.coli. These proteins mediate the periodic inversion of a 300bp DNA segment that harbors the promoter for the fimbrial structural gene, FimA. FimB switches FimA on. (200 aa)
fimAMajor type 1 subunit fimbrin (pilin); Fimbriae (also called pili), polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, enable bacteria to colonize the epithelium of specific host organs. (182 aa)
trmItRNA m(7)G46 methyltransferase, SAM-dependent; Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA; Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family. (239 aa)
recADNA recombination and repair protein; Required for homologous recombination and the bypass of mutagenic DNA lesions by the SOS response. Catalyzes ATP-driven homologous pairing and strand exchange of DNA molecules necessary for DNA recombinational repair. Catalyzes the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single- stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. The SOS response controls an apoptotic-like death (ALD) induced (in the absence of the mazE-mazF toxin-antitoxin module) in resp [...] (353 aa)
yfjYCP4-57 prophage; Putative DNA repair protein; Belongs to the UPF0758 family. (160 aa)
yfaLAdhesin; Probably an autotransporter. (1250 aa)
yeeSCP4-44 prophage; Putative DNA repair protein, RADC family; Belongs to the UPF0758 family. (148 aa)
fluNovel sRNA, CP4-44; Controls colony form variation and autoaggregation. May function as an adhesin. (1039 aa)
fumCFumarate hydratase (fumarase C),aerobic Class II; Involved in the TCA cycle. FumC seems to be a backup enzyme for FumA under conditions of iron limitation and oxidative stress. Catalyzes the stereospecific interconversion of fumarate to L-malate. Belongs to the class-II fumarase/aspartase family. Fumarase subfamily. (467 aa)
ompWOuter membrane protein W; Acts as a receptor for colicin S4. (212 aa)
hlyEHemolysin E; Toxin, which has some hemolytic activity towards mammalian cells. Acts by forming a pore-like structure upon contact with mammalian cells. (303 aa)
sfmAFimA homolog, function unknown; Part of the sfmACDHF fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches. Increases adhesion to eukaryotic T24 bladder epithelial cells in the absence of fim genes. (180 aa)
hhaModulator of gene expression, with H-NS; Down-regulates hemolysin (hly) expression in complex with H- NS. Stimulates transposition events in vivo. Modifies the set of genes regulated by H-NS; Hha and Cnu (YdgT) increase the number of genes DNA bound by H-NS/StpA and may also modulate the oligomerization of the H-NS/StpA-complex. Binds DNA and influences DNA topology in response to environmental stimuli; does not however interact with DNA in the absence of H-NS. Involved in persister cell formation, acting downstream of mRNA interferase (toxin) MqsR. Decreases biofilm formation by repre [...] (72 aa)
ykfGCP4-6 prophage; Putative DNA repair protein; Belongs to the UPF0758 family. (158 aa)
btuBVitamin B12/cobalamin outer membrane transporter; Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans- periplasmic membrane protein TonB. Is also a receptor for bacteriophages BF23 and C1, and for A and E colicins. (614 aa)
dctRPutative LuxR family repressor for dicarboxylate transport; May act as a transcriptional regulator of dctA. (176 aa)
yhiDPutative Mg(2+) transport ATPase, inner membrane protein; Could be involved in magnesium uptake. (215 aa)
hdeDAcid-resistance membrane protein. (190 aa)
gadEGad regulon transcriptional activator; Regulates the expression of several genes involved in acid resistance. Required for the expression of gadA and gadBC, among others, regardless of media or growth conditions. Binds directly to the 20 bp GAD box found in the control regions of both loci. (175 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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