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grpE protein (Porphyromonas gingivalis W83) - STRING interaction network
grpE protein in Porphyromonas gingivalis W83
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second shell of interactors
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proteins of unknown 3D structure
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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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 [...] (194 aa)    
Predicted Functional Partners:
dnaJ
dnaJ protein; 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, DnaK and Gr [...] (383 aa)
 
  0.999
dnaK
dnaK protein; Acts as a chaperone (640 aa)
 
  0.998
groL
Chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (545 aa)
   
  0.973
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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity) (863 aa)
   
 
  0.933
groS
Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (89 aa)
 
 
  0.920
clpC
ATP-dependent Clp protease, ATP-binding subunit ClpC (859 aa)
   
 
  0.916
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 (673 aa)
   
  0.866
PG_0509
Phosphoribose diphosphate-decaprenyl-phosphate phosphoribosyltransferase (286 aa)
   
 
    0.808
tkt
Transketolase (675 aa)
       
  0.801
htpG
Heat shock protein 90; Molecular chaperone. Has ATPase activity (684 aa)
     
   
  0.800
Your Current Organism:
Porphyromonas gingivalis W83
NCBI taxonomy Id: 242619
Other names: P. gingivalis W83, Porphyromonas gingivalis W83, Porphyromonas gingivalis str. W83, Porphyromonas gingivalis strain W83
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