STRING protein interaction network
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:
some 3D structure is known or predicted
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
protein homology
Your Input:
Gene Fusion
cpxPActs as an auxiliary protein in the Cpx two-component envelope stress response system, helping modulate the Cpx response systems response to some inducers . Binds the periplasmic domain of sensor histidine kinase CpxA, inhibiting induction of the Cpx envelope stress response in the absence of inducer; overexpression decreases Cpx pathway activity . Some periplasmic stimulii (shown for P pili subunit PapE and probably 0.3 M NaCl) increase CpxP's susceptibility to DegP, leading to CpxP degradation, inducing the Cpx pathway . Aids in combating extracytoplasmic protein-mediated toxicity Ov [...] (166 aa)    
Predicted Functional Partners:
Histidine kinase 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 . Activates CpxR by phosphorylation; has autokinase, phosphotransferase and (in the presence of Mg(2+) and/or ATP or ADP) phosphatase activity . The kinase activity is inhibited by periplasmic accessory protein CpxP; proteolysis of CpxP relieves inhibition Involved in several diverse cellular processes, including the functioning of acetohydroxyacid synthetase I, the biosynthesis of isoleucine [...]
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 enhanced by phosphorylation . This system combats a variety of extr [...]
Serine 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 protei [...]
Lipoprotein involved with copper homeostasis and adhesion; Involved in copper homeostasis, could be involved in both copper efflux and the delivery of copper to copper-dependent enzymes . Required for efficient binding of stationary phase cells to hydrophobic surfaces, part of the process of biofilm formation . Functions during envelope stress responses; when overproduced induces degP through the activation of the two-component envelope stress response system CpxA/CpxR DegP induction seems to require membrane anchoring of this protein . Structural changes and/or interaction of the CXXC [...]
An anti-sigma factor for extracytoplasmic function (ECF) sigma factor sigma-E (RpoE). ECF sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis (RIP). RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein is first cut periplasmically (site-1 protease, S1P, DegS), then within the membrane itself (site-2 protease, S2P, RseP), while cytoplasmic proteases finish degrading the anti-sigma fac [...]
Rna polymerase sigma-70 factor, ecf subfamily; Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released Extracytoplasmic function (ECF) sigma-E controls the envelope stress response, responding to periplasmic protein stress, increased levels of periplasmic lipopolysaccharide (LPS) as well as heat shock and oxidative stress; it controls protein processing in the extracytoplasmic compartment. The 90 member regulon consists of the genes necessary for the synthesis and maintenance of both proteins and LPS o [...]
annotation not available
Outer membrane protein assembly factor bamc; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex that stabilizes the interaction between the essential proteins BamA and BamD. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly [...]
Outer membrane porin protein c; Forms pores that allow passive diffusion of small molecules across the outer membrane. (Microbial infection) A mixed OmpC-OmpF heterotrimer is the outer membrane receptor for toxin CdiA-EC536; polymorphisms in extracellular loops 4 and 5 of OmpC confer susceptibility to CdiA- EC536-mediated toxicity
Protein that modulates hha toxicity; Attenuates Hha toxicity and regulates biofilm formation. Binds to various coding and intergenic regions of genomic DNA
Your Current Organism:
Escherichia coli K12 MG1655
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli K12 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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