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
Your Input:
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Gene Fusion
Cooccurrence
Coexpression
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[Homology]
Score
grpEGrpE protein; 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 [...] (197 aa)    
Predicted Functional Partners:
dnaK-2
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.992
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.984
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.983
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 [...]
 
 
 0.974
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.
  
  
 0.973
Deba_0163
COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterProIPR001623:IPR002939:IPR008971:IPR018253:IPR 003095; KEGG: sat:SYN_00894 chaperone protein; PFAM: chaperone DnaJ domain protein; heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; SPTR: Q2LTT1 Chaperone protein; PFAM: DnaJ domain; DnaJ C terminal region.
 
 
 0.964
Deba_3031
KEGG: gvi:glr2966 hypothetical protein; SPTR: Q7NCL2 Glr2966 protein.
  
 0.953
groS
Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 
 0.945
clpB
ATP-dependent 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.
  
 
 0.907
Deba_3296
InterPro IPR001623:IPR003095; KEGG: cce:Ccel_1797 chaperone protein DnaJ; PFAM: heat shock protein DnaJ domain protein; SPTR: B9XFY3 Chaperone protein dnaJ; PFAM: DnaJ domain.
  
 
 0.903
Your Current Organism:
Desulfarculus baarsii
NCBI taxonomy Id: 644282
Other names: D. baarsii DSM 2075, Desulfarculus baarsii 2st 14, Desulfarculus baarsii DSM 2075, Desulfarculus baarsii str. DSM 2075, Desulfarculus baarsii strain DSM 2075
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