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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from curated databases
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Assay-based Predictions
experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
AEN97429.1COG0443 Molecular chaperone; Belongs to the heat shock protein 70 family. (636 aa)    
Predicted Functional Partners:
grpE
Molecular chaperone GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. 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 [...]
 
 
 0.981
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 [...]
 0.975
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.965
AEN96346.1
Heat shock protein 90; COG0326 Molecular chaperone, HSP90 family.
   
 0.944
AEN96113.1
Heat shock protein DnaJ domain-containing protein; COG2214 DnaJ-class molecular chaperone.
 
 0.935
groS
Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.889
AEN97428.1
COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain.
 
     0.854
hrcA
Heat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons.
  
  
 0.827
AEN95540.1
ICESt1 ORFD ATP/GTP-binding protein; COG0542 ATPases with chaperone activity, ATP-binding subunit.
 
 
 0.816
AEN95236.1
Hypothetical protein.
  
 0.792
Your Current Organism:
Roseburia hominis
NCBI taxonomy Id: 585394
Other names: R. hominis A2-183, Roseburia hominis A2-183, Roseburia hominis str. A2-183, Roseburia hominis strain A2-183, butyrate-producing bacterium A2-183
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