STRINGSTRING
grpE protein (Sulfurovum sp. NBC371) - STRING interaction network
"grpE" - Co-chaperone protein GrpE in Sulfurovum sp. NBC371
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 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
grpECo-chaperone protein 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 AT [...] (184 aa)    
Predicted Functional Partners:
dnaK
Chaperone protein DnaK; Acts as a chaperone (627 aa)
 
  0.999
dnaJ
Co-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 [...] (377 aa)
 
 
  0.992
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (542 aa)
 
  0.983
SUN_1562
Co-chaperone-curved DNA binding protein A (291 aa)
 
  0.936
clpA
ATP-dependent Clp protease, ATP-binding subunit ClpA (729 aa)
   
 
  0.931
clpB
ATP-dependent Clp protease, ATP-binding subunit ClpB (857 aa)
   
 
  0.931
groS
Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (86 aa)
   
 
  0.928
ftsH
Cell division protein FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins (671 aa)
   
  0.870
SUN_0166
Transketolase; Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate (659 aa)
       
  0.796
SUN_1099
ATP-dependent M41 family peptidase (448 aa)
   
  0.788
Your Current Organism:
Sulfurovum sp. NBC371
NCBI taxonomy Id: 387093
Other names: S. sp. NBC37-1, Sulfurovum, Sulfurovum Inagaki et al. 2004, Sulfurovum NBC37_1, Sulfurovum sp. NBC37-1, Sulfurovum sp. NBC371
Server load: low (12%) [HD]