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 co-occurrence
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htpGChaperone protein htpG; Molecular chaperone. Has ATPase activity. (615 aa)    
Predicted Functional Partners:
groL
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
 
 0.969
AEJ60430.1
Peptidoglycan-binding lysin domain-containing protein; PFAM: LysM domain; InterPro IPR018392:IPR002482; KEGG: sta:STHERM_c01550 hypothetical protein; PFAM: Peptidoglycan-binding lysin domain; SMART: Peptidoglycan-binding Lysin subgroup; SPTR: Peptidoglycan-binding lysin domain.
  
 0.937
AEJ62118.1
KEGG: sta:STHERM_c17890 hypothetical protein; SPTR: Putative uncharacterized protein.
  
 0.937
dnaK
Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
 0.937
hslV
ATP-dependent protease hslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
   
  
 0.901
groS
10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
   
 
 0.895
hslU
ATP-dependent hsl protease ATP-binding subunit hslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
   
  
 0.894
AEJ60847.1
Heat shock protein DnaJ domain protein; PFAM: DnaJ domain; InterPro IPR001623; KEGG: sta:STHERM_c05450 hypothetical protein; PFAM: Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal; SPTR: Heat shock protein DnaJ domain protein.
  
 0.879
AEJ61281.1
Heat shock protein DnaJ domain protein; PFAM: DnaJ domain; COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterPro IPR001623; KEGG: sta:STHERM_c09840 molecular chaperone protein; PFAM: Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal; SPTR: Heat shock protein DnaJ domain protein.
  
 0.879
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 [...]
  
 0.879
Your Current Organism:
Spirochaeta thermophila
NCBI taxonomy Id: 869211
Other names: S. thermophila DSM 6578, Spirochaeta thermophila DSM 6578, Spirochaeta thermophila str. DSM 6578, Spirochaeta thermophila strain DSM 6578
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