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htpG protein (Porphyromonas gingivalis W83) - STRING interaction network
"htpG" - Heat shock protein 90 in Porphyromonas gingivalis W83
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Edges represent protein-protein associations
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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
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
htpGHeat shock protein 90; Molecular chaperone. Has ATPase activity (684 aa)    
Predicted Functional Partners:
dnaK
dnaK protein; Acts as a chaperone (640 aa)
     
  0.982
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)
   
  0.963
groL
Chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (545 aa)
     
 
  0.936
groS
Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (89 aa)
     
 
  0.930
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)
   
 
  0.913
PG_1864
Leucine-rich protein (1266 aa)
       
  0.912
PG_1374
Hypothetical protein (428 aa)
       
  0.912
PG_0350
Internalin-like protein (484 aa)
       
  0.912
clpC
ATP-dependent Clp protease, ATP-binding subunit ClpC (859 aa)
   
 
  0.878
PG_2200
Hypothetical protein (695 aa)
   
  0.862
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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