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groL protein (Pseudoflavonifractor capillosus) - STRING interaction network
"groL" - 60 kDa chaperonin in Pseudoflavonifractor capillosus
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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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Score
groL60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (542 aa)    
Predicted Functional Partners:
groS
10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (94 aa)
 
  0.999
grpE
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 ATP- dependent [...] (188 aa)
 
  0.979
EDM99392.1
Chaperone protein DnaK; Acts as a chaperone (619 aa)
 
  0.919
htpG
Chaperone protein HtpG; Molecular chaperone. Has ATPase activity (642 aa)
     
 
  0.916
EDN00755.1
Chaperone protein DnaK; Acts as a chaperone (572 aa)
 
  0.916
EDM99289.1
DnaK family protein; KEGG- mbo-Mb0358 1.2e-46 dnaK; probable chaperone protein DnaK (heat shock protein 70) (heat shock 70 kda protein) (HSP70) K04043; COG- COG0443 Molecular chaperone; Psort location- Cytoplasmic, score-9.26 (437 aa)
 
  0.904
EDN00092.1
ATP-dependent Clp protease proteolytic subunit; 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 (193 aa)
 
 
  0.893
clpX
ATP-dependent Clp protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (438 aa)
 
   
  0.881
guaB
Inosine-5’-monophosphate dehydrogenase; Catalyzes the conversion of inosine 5’-phosphate (IMP) to xanthosine 5’-phosphate (XMP), the first committed and rate- limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth; Belongs to the IMPDH/GMPR family (491 aa)
   
 
  0.860
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 [...] (387 aa)
 
  0.851
Your Current Organism:
Pseudoflavonifractor capillosus
NCBI taxonomy Id: 411467
Other names: Bacteroides capillosus ATCC 29799, P. capillosus ATCC 29799, Pseudoflavonifractor capillosus, Pseudoflavonifractor capillosus ATCC 29799, Pseudoflavonifractor capillosus ATCC29799, Pseudoflavonifractor capillosus str. ATCC 29799, Pseudoflavonifractor capillosus strain ATCC 29799
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