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dnaJ protein (Porphyromonas gingivalis W83) - STRING interaction network
dnaJ protein in Porphyromonas gingivalis W83
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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
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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dnaJdnaJ 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)    
Predicted Functional Partners:
dnaK
dnaK protein; Acts as a chaperone (640 aa)
 
  0.999
grpE
grpE 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)
 
  0.999
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)
   
  0.988
clpC
ATP-dependent Clp protease, ATP-binding subunit ClpC (859 aa)
   
  0.988
htpG
Heat shock protein 90; Molecular chaperone. Has ATPase activity (684 aa)
   
  0.963
groL
Chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (545 aa)
 
  0.961
prmA
Ribosomal protein L11 methyltransferase; Methylates ribosomal protein L11 (311 aa)
   
   
  0.870
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)
   
  0.863
PG_0196
M16 family peptidase (941 aa)
   
  0.845
PG_0088
M16 family peptidase (405 aa)
   
  0.845
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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