STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
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
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
htpGChaperonine hsp90 protein; Molecular chaperone. Has ATPase activity. (643 aa)    
Predicted Functional Partners:
dnaK
DNAK Protein; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.959
Avi_3078
Possible heat shock protein.
 
 0.956
Avi_1385
Molecular chaperone Hsp70 family.
  
 0.938
groEL
Chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
 
 0.926
dnaJ
Molecular chaperone DnaJ family; 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 betwee [...]
 
 0.897
Avi_2744
Conserved hypothetical protein.
  
 0.890
groES
10 KD chaperonin (protein CPN10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
   
 
 0.889
hslV
Heat shock protein hslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
   
  
 0.882
hslU
Heat shock chaperone; 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.
   
  
 0.878
dnaJ-3
Molecular chaperone DnaJ family.
  
 0.875
Your Current Organism:
Agrobacterium vitis
NCBI taxonomy Id: 311402
Other names: A. vitis S4, Agrobacterium vitis S4, Agrobacterium vitis str. S4, Agrobacterium vitis strain S4
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.