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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experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
AEE51460.1ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity. (622 aa)    
Predicted Functional Partners:
AEE48774.1
COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterPro IPR001623:IPR002939; KEGG: fjo:Fjoh_2374 chaperone DnaJ domain-containing protein; PFAM: Chaperone DnaJ, C-terminal; Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal; SPTR: Chaperone DnaJ domain protein; IMG reference gene:2504770230; PFAM: DnaJ domain; DnaJ C terminal region.
  
 0.850
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 [...]
  
 0.850
groL
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
 
 0.842
groL-2
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
 
 0.842
AEE52920.1
Heat shock protein 70; COGs: COG0443 Molecular chaperone; InterPro IPR013126; KEGG: sli:Slin_5724 TIR protein; PFAM: Heat shock protein 70; SPTR: TIR protein; IMG reference gene:2504774492; PFAM: Hsp70 protein.
   
 0.836
AEE52926.1
Heat shock protein; COGs: COG0443 Molecular chaperone; KEGG: chu:CHU_2145 heat shock protein; SPTR: Probable heat shock protein; IMG reference gene:2504774498; PFAM: Hsp70 protein.
   
 0.836
AEE53655.1
Heat shock protein 70; COGs: COG0443 Molecular chaperone; InterPro IPR013126; KEGG: phe:Phep_3231 Fe-S protein assembly chaperone HscA; PFAM: Heat shock protein 70; SPTR: Heat shock protein 70; IMG reference gene:2504775230; PFAM: Hsp70 protein; TIGRFAM: Fe-S protein assembly chaperone HscA.
   
 0.836
dnaK
Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
   
 0.836
groS
10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
   
 
 0.788
grpE
Protein 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-dependent i [...]
 
 
 0.781
Your Current Organism:
Haliscomenobacter hydrossis
NCBI taxonomy Id: 760192
Other names: H. hydrossis DSM 1100, Haliscomenobacter hydrossis DSM 1100
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