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:
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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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Gene Fusion
Cooccurrence
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[Homology]
Score
grpEProtein grpE (HSP-70 cofactor); 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 [...] (222 aa)    
Predicted Functional Partners:
dnaK
Chaperone protein dnaK (Heat shock protein 70); Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.999
groEL
groEL protein; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 0.992
groES
groES protein; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.981
hrcA
Heat-inducible transcription repressor hrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons.
  
  
 0.977
BAD_1545
Chaperone protein similar to DnaJ; COG family: molecular chaperones (containC-terminal Zn finger domain); Orthologue of BL0517; PFAM_ID: DnaJ; PFAM_ID:DnaJ_C.
 
 
 0.970
BAD_1544
Probable MerR-type-transcriptional regulator; COG family: predicted transcriptional regulators; Orthologue of BL0516; PFAM_ID: merR.
  
  
 0.961
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 [...]
 
 
 0.951
clpC1
Orthologue of Rv3596c_BL0010; ProbableclpC1_ ATP-dependent protease ATP-binding subunit (EC3.4.-.-); Belongs to the ClpA/ClpB family.
  
 
 0.824
clpB
Chaperone clpB; 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.
  
 
 0.824
clp1
ATP-dependent Clp protease proteolytic subunit 2; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.
   
 
 0.739
Your Current Organism:
Bifidobacterium adolescentis
NCBI taxonomy Id: 367928
Other names: B. adolescentis ATCC 15703, Bifidobacterium adolescentis ATCC 15703, Bifidobacterium adolescentis str. ATCC 15703, Bifidobacterium adolescentis strain ATCC 15703
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.