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dnaK protein (Vibrio vulnificus) - STRING interaction network
"dnaK" - Chaperone protein DnaK in Vibrio vulnificus
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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
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some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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dnaKChaperone protein DnaK; Acts as a chaperone (636 aa)    
Predicted Functional Partners:
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 [...] (198 aa)
 
  0.999
VV0833
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 [...] (381 aa)
 
  0.999
clpB
Chaperone protein 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. 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); Belongs to the ClpA/ClpB family (857 aa)
 
 
  0.989
groL1
60 kDa chaperonin 1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (546 aa)
 
 
  0.981
groL2
60 kDa chaperonin 2; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (532 aa)
 
 
  0.981
htpG
Chaperone protein HtpG; Molecular chaperone. Has ATPase activity (634 aa)
   
 
  0.976
groS1
10 kDa chaperonin 1; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (96 aa)
 
 
  0.937
groS2
10 kDa chaperonin 2; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (96 aa)
 
 
  0.935
hslU
ATP-dependent protease ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis (443 aa)
   
 
  0.916
hslV
ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery (184 aa)
   
 
  0.912
Your Current Organism:
Vibrio vulnificus
NCBI taxonomy Id: 672
Other names: ATCC 27562, BCRC 12905, Beneckea vulnifica, CAIM 610, CCRC 12905, CCUG 13448, CCUG 16394, CIP 75.4, DSM 10143, IFO 15645, JCM 3725, LMG 13545, NBRC 15645, V. vulnificus, Vibrio vulnificus, strain 324
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