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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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textmining
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experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
KUN45443.1Molecular chaperone HtpG; Derived by automated computational analysis using gene prediction method: Protein Homology. (612 aa)    
Predicted Functional Partners:
groEL-2
Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
 0.973
groEL
Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
 0.972
KUN45442.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
   
 0.966
dnaK
Fe-S protein assembly chaperone HscA; Acts as a chaperone; Belongs to the heat shock protein 70 family.
   
 0.954
dnaK-2
Fe-S protein assembly chaperone HscA; Acts as a chaperone; Belongs to the heat shock protein 70 family.
   
 0.954
dnaK_2
Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
   
 0.948
dnaJ1
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, [...]
  
 0.941
dnaK_1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.931
dnaJ2
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, [...]
  
 0.898
KUN44025.1
Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.898
Your Current Organism:
Streptomyces olivochromogenes
NCBI taxonomy Id: 1963
Other names: ATCC 25479, ATCC 3336, Actinomyces olivochromogenus, CBS 889.69, DSM 40451, IFO 13067, IFO 3178, IMET 40352, ISP 5451, JCM 4163, JCM 4500, KCTC 9064, NBRC 13067, NBRC 3178, NRRL-ISP 5451, S. olivochromogenes, Streptomyces olivichromogenes, Streptomyces olivochromogenus
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