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glr4267 protein (Gloeobacter violaceus) - STRING interaction network
"glr4267" - Molecular chaperone DnaJ in Gloeobacter violaceus
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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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glr4267Molecular chaperone 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, [...] (383 aa)    
Predicted Functional Partners:
glr4264
Molecular chaperone DnaK; Acts as a chaperone (638 aa)
 
  0.999
gll3802
Hypothetical protein (511 aa)
 
  0.998
gll1676
Molecular chaperone DnaK (525 aa)
 
  0.998
grpE
Heat shock 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- depe [...] (196 aa)
 
 
  0.986
clpB
Endopeptidase Clp ATP-binding chain B; 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) (872 aa)
   
 
  0.909
glr2064
Endopeptidase Clp ATP-binding chain (819 aa)
   
 
  0.909
glr1542
Endopeptidase Clp ATP-binding chain (778 aa)
   
 
  0.909
clpC
ATP-dependent protease ATP-binding subunit (727 aa)
   
 
  0.870
gll2588
Endopeptidase Clp ATP-binding chain (348 aa)
   
 
  0.870
gll2068
Endopeptidase Clp ATP-binding chain (330 aa)
   
 
  0.870
Your Current Organism:
Gloeobacter violaceus
NCBI taxonomy Id: 251221
Other names: G. violaceus, G. violaceus PCC 7421, Gloeobacter, Gloeobacter violaceus, Gloeobacter violaceus ATCC 29082, Gloeobacter violaceus PCC 7421, Gloeobacter violaceus str. PCC 7421, Gloeobacter violaceus strain PCC 7421, Gloeobacterales, Gloeobacterales Cavalier-Smith 2002, Gloeobacteria, Gloeobacteria Cavalier-Smith 2002
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