STRINGSTRING
fimA fimA lacZ lacZ sfmC sfmC sfmH sfmH sfmF sfmF ompA ompA flhA flhA fliC fliC fliD fliD fliS fliS flu flu lrhA lrhA crp crp bax bax fimB fimB fimE fimE fimI fimI fimC fimC fimF fimF fimH fimH
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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
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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:
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)
lacZbeta-D-galactosidase; Protein involved in carbohydrate catabolic process; Belongs to the glycosyl hydrolase 2 family. (1024 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)
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)
sfmFFimA 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. (171 aa)
ompAOuter membrane protein A (3a;II*;G;d); With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm (Probable). Plays a role in resistance to environmental stress, and a role in outer membrane functionality and cell shape. Non-covalently binds peptidoglycan (Probable). Acts as a porin with low permeability that allows slow penetration of small solutes. A very abundant protein, there can be up to 210,000 OmpA molecules per cell. Reconstitution in unilamellar lipid vesicles shows only about 3% of the protein is in an open conformation, whic [...] (346 aa)
flhAPutative flagellar export pore protein; Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin; Belongs to the FHIPEP (flagella/HR/invasion proteins export pore) family. (692 aa)
fliCFlagellar filament structural protein (flagellin); Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (498 aa)
fliDFlagellar filament capping protein; Required for the morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end; Belongs to the FliD family. (468 aa)
fliSFlagellar biosynthesis; repressor of class 3a and 3b operons (RflA activity); Protein involved in flagellum assembly and taxis. (136 aa)
fluNovel sRNA, CP4-44; Controls colony form variation and autoaggregation. May function as an adhesin. (1039 aa)
lrhATranscriptional repressor of flagellar, motility and chemotaxis genes; Not known, does not seem to act on the proton translocating NADH dehydrogenase genes (nuoA-N) which are part of the lrhA operon. (312 aa)
crpcAMP-activated global transcription factor, mediator of catabolite repression; A global transcription regulator. Complexes with cyclic AMP (cAMP) which allosterically activates DNA binding (to consensus sequence 5'-AAATGTGATCTAGATCACATTT-3') to directly regulate the transcription of about 300 genes in about 200 operons and indirectly regulate the expression of about half the genome. There are 3 classes of CRP promoters; class I promoters have a single CRP-binding site upstream of the RNA polymerase (RNAP)-binding site, whereas in class II promoters the single CRP- and RNAP-binding site [...] (210 aa)
baxPutative ATP-binding protein. (274 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)
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)
fimFMinor 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). Involved in the integration of FimH in the fimbriae; Belongs to the fimbrial protein family. (176 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)
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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