STRINGSTRING
sfmH sfmH degP degP dksA dksA araC araC lrp lrp atpF atpF atpE atpE dam dam atpB atpB atpG atpG atpD atpD atpC atpC dsbA dsbA cpxR cpxR fimB fimB fimE fimE fimA fimA bax bax atpH atpH fimI fimI fimC fimC fimH fimH fabZ fabZ sfmA sfmA focA focA sfmC sfmC
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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:
sfmHFimA 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. (327 aa)
degPSerine endoprotease (protease Do), membrane-associated; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. Degrades transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. [...] (474 aa)
dksATranscriptional regulator of rRNA transcription; Transcription factor that acts by binding directly to the RNA polymerase (RNAP). Required for negative regulation of rRNA expression and positive regulation of several amino acid biosynthesis promoters. Also required for regulation of fis expression. Binding to RNAP disrupts interaction of RNAP with DNA, inhibits formation of initiation complexes, and amplifies effects of ppGpp and the initiating NTP on rRNA transcription. Inhibits transcript elongation, exonucleolytic RNA cleavage and pyrophosphorolysis, and increases intrinsic terminat [...] (151 aa)
araCAra regulon transcriptional activator; Transcription factor that regulates the expression of several genes involved in the transport and metabolism of L-arabinose. Functions both as a positive and a negative regulator. In the presence of arabinose, activates the expression of the araBAD, araE, araFGH and araJ promoters. In the absence of arabinose, negatively regulates the araBAD operon. Represses its own transcription. Acts by binding directly to DNA. (292 aa)
lrpLeucine-responsive global transcriptional regulator; Mediates a global response to leucine. Exogenous leucine affects the expression of a number of different operons; lrp mediates this effect for at least some of these operons. For example it is regulator of the branched-chain amino acid transport genes. (164 aa)
atpFF0 sector of membrane-bound ATP synthase, subunit b; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (156 aa)
atpEF0 sector of membrane-bound ATP synthase, subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (79 aa)
damDNA adenine methyltransferase; Methylates DNA within the sequence GATC and protects the DNA from cleavage by the restriction endonuclease MboI. Although it shares sequence specificity with a number of type II restriction endonucleases and methylases, it is thought to act in postreplication mismatch repair rather than as a part of a restriction modification system. May also play a role in DNA replication. (278 aa)
atpBF0 sector of membrane-bound ATP synthase, subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. (271 aa)
atpGF1 sector of membrane-bound ATP synthase, gamma subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. (287 aa)
atpDF1 sector of membrane-bound ATP synthase, beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. (460 aa)
atpCF1 sector of membrane-bound ATP synthase, epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane; Belongs to the ATPase epsilon chain family. (139 aa)
dsbAPeriplasmic protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. Required for pilus biogenesis. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. Belongs to the thioredoxin family. DsbA subfamily. (208 aa)
cpxRResponse regulator in two-component regulatory system with CpxA; Response regulator member of the two-component regulatory system CpxA/CpxR which responds to envelope stress response by activating expression of downstream genes including cpxP, degP, dsbA and ppiA. Required for efficient binding of stationary phase cells to hydrophobic surfaces, part of the process of biofilm formation. Induced upon cell surface binding, subsequently induces genes it controls (cpxP, dsbA and spy, degP is only partially induced). Binds and activates transcription from the degP promoter ; binding is enhan [...] (232 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)
fimETyrosine recombinase/inversion of on/off regulator of fimA; FimE 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. FimE switches fimA off. (198 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)
baxPutative ATP-binding protein. (274 aa)
atpHF1 sector of membrane-bound ATP synthase, delta subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family. (177 aa)
fimIFimbrial protein; Protein involved in glycoprotein biosynthetic process. (179 aa)
fimCPeriplasmic chaperone; Required for the biogenesis of type 1 fimbriae. Binds and interact with FimH. (241 aa)
fimHMinor component of type 1 fimbriae; Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Adhesin responsible for the binding to D-mannose. It is laterally positioned at intervals in the structure of the type 1 fimbriae. In order to integrate FimH in the fimbriae FimF and FimG are needed. (300 aa)
fabZ(3R)-hydroxymyristol acyl carrier protein dehydratase; Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs. (151 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)
focAFormate channel; Involved in the bidirectional transport of formate; Belongs to the FNT transporter (TC 2.A.44) family. (285 aa)
sfmCPutative periplasmic pilus chaperone; 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. (230 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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