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
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
htpGHeat-shock protein Hsp90; Molecular chaperone. Has ATPase activity. (636 aa)    
Predicted Functional Partners:
dnaK
Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
   
 0.964
OOQ49222.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.954
groEL
Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
 0.936
groEL-2
Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
 0.935
dnaJ-2
Molecular chaperone 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, [...]
  
 0.902
dnaJ
Molecular chaperone 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, [...]
  
 0.878
OOQ52015.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.864
OOQ52380.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.859
OOQ52761.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.834
OOQ51159.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.834
Your Current Organism:
Streptomyces antibioticus
NCBI taxonomy Id: 1890
Other names: ATCC 23879, ATCC 8663, Actinomyces antibioticus, BCRC 12164, CBS 478.48, CBS 659.68, CCM 3159, CCRC 12164, CCRC:12164, CECT 3225, DSM 40234, IFO 12838, IMET 40227, ISP 5234, JCM 4620, KCTC 9688, LMG 5966, LMG:5966, NBRC 12838, NCIMB 8504, NRRL B-2770, NRRL-ISP 5234, S. antibioticus, Streptomyces antibioticus subsp. antibioticus, VKM Ac-964
Server load: low (12%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.