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:
a 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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
grpE_2Protein GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent i [...] (234 aa)    
Predicted Functional Partners:
dnaK_1
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.999
groEL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 0.992
groES
10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.983
DnaJ
DnaJ-class molecular chaperone.
 
 
 0.976
dnaJ
Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...]
 
 
 0.975
HrcA
HrcA Heat-inducible transcription repressor.
  
  
 0.928
clpB
ClpB protein; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family.
  
 
 0.919
HspR
Putative heat shock protein.
  
  
 0.905
clpC
ClpC; Belongs to the ClpA/ClpB family.
  
 
 0.841
RY70_26
Cell surface protein with gram positive anchor domain.
  
 
 0.785
Your Current Organism:
Bifidobacterium bifidum
NCBI taxonomy Id: 1681
Other names: AS 1.2212, ATCC 29521, Actinobacterium bifidum, Actinomyces bifidus, Actinomyces parabifidus, B. bifidum, BCRC 14615, Bacillus bifidus, Bacillus bifidus communis, Bacterium bifidum, Bacteroides bifidus, Bifidibacterium bifidum, CCRC 14615, CCRC:14615, CCUG 18364, CCUG 45217, CIP 56.7, Cohnistreptothrix bifidus, DSM 20456, IFO 14252, KCTC 3202, LMG 11041, LMG 8810, LMG:11041, LMG:8810, Lactobacillus bifidus type II, Lactobacillus parabifidus, NBRC 100015, NBRC 14252, NCFB 2715, NCIMB 702715, NCTC 13001, Nocardia bifida, Tissieria bifida, strain Ti
Server load: low (12%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.