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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
htpGHeat shock protein 90; Molecular chaperone. Has ATPase activity. (631 aa)    
Predicted Functional Partners:
dnaJ
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 [...]
 
 0.884
dnaJ-2
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 [...]
 
 0.876
RAM_26330
Chaperone protein DnaK-like protein; COG0443 Molecular chaperone; Belongs to the heat shock protein 70 family.
 
 0.828
RAM_39810
Hypothetical protein.
    
 0.825
dnaK
Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.825
groS
Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
   
 
 0.816
DnaK-2
Molecular chaperone DnaK; COG4249 Uncharacterized protein containing caspase domain; Belongs to the heat shock protein 70 family.
 
 0.807
RAM_17080
Hypothetical protein; COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain.
  
 0.801
HscA
COG0443 Molecular chaperone; Belongs to the heat shock protein 70 family.
  
 0.799
RAM_07555
COG0443 Molecular chaperone.
  
 0.799
Your Current Organism:
Amycolatopsis mediterranei
NCBI taxonomy Id: 713604
Other names: A. mediterranei S699, Amycolatopsis mediterranei S699, Amycolatopsis mediterranei str. S699, Amycolatopsis mediterranei strain S699
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.