STRINGSTRING
STRING protein interaction network
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:
some 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:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
pphAPlays a key role in signaling protein misfolding via the CpxR/CPXA transducing system. It also modulates the phosphorylated status of many phosphoproteins in E.coli, some of which acting as major chaperones. Has been shown, in vitro, to act on Ser, Thr and Tyr- phosphorylated substrates (218 aa)    
Predicted Functional Partners:
yebY
annotation not available
     
 0.748
htpG
Molecular chaperone. Has ATPase activity
    
 0.549
yebZ
Inner membrane protein YebZ; Putative resistance protein; Protein involved in response to drug
 
     0.544
degP
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 . Its proteolytic activity is essential for the survi [...]
    
 0.521
fkpA
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides
   
 0.521
fklB
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides
   
 0.521
yrbL
annotation not available
  
 0.487
waaP
Catalyzes the phosphorylation of heptose(I) of the outer membrane lipopolysaccharide core
  
 0.487
mdtN
Could be involved in resistance to puromycin, acriflavine and tetraphenylarsonium chloride
   
  
 0.486
yobA
annotation not available
 
     0.457
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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