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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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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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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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co-expression
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[Homology]
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htpGHeat shock protein Hsp90; Molecular chaperone. Has ATPase activity. (630 aa)    
Predicted Functional Partners:
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
   
 0.993
ADW17100.1
Peptidylprolyl isomerase; COGs: COG0652 Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family; InterPro IPR002130: IPR001179: IPR020892; KEGG: dps:DP1645 peptidyl-prolyl cis-trans isomerase; PFAM: peptidyl-prolyl cis-trans isomerase cyclophilin type; peptidylprolyl isomerase FKBP-type; PRIAM: Peptidylprolyl isomerase; SPTR: Probable peptidyl-prolyl cis-trans isomerase; PFAM: FKBP-type peptidyl-prolyl cis-trans isomerase; Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD.
  
 0.992
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
 
 0.975
ADW18122.1
COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterProIPR003095: IPR012724: IPR018253: IPR001623: IPR 001305: IPR002939; KEGG: dps:DP1482 chaperone protein DnaJ; PFAM: chaperone DnaJ domain protein; heat shock protein DnaJ domain protein; DnaJ central domain protein; SMART: heat shock protein DnaJ domain protein; SPTR: Chaperone protein dnaJ; TIGRFAM: chaperone protein DnaJ; PFAM: DnaJ domain; DnaJ central domain (4 repeats); DnaJ C terminal region; TIGRFAM: chaperone protein DnaJ.
  
 0.965
clpB
ATP-dependent chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family.
  
 
 0.938
hslV
ATP dependent peptidase CodWX, CodW component; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
   
  
 0.907
hslU
Heat shock protein HslVU, ATPase 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.
   
  
 0.901
groS
Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
   
 
 0.885
clpA
ATP-dependent Clp protease ATP-binding subunit ClpA; COGs: COG0542 ATPase with chaperone activity ATP-binding subunit; InterProIPR004176: IPR003959: IPR013093: IPR019489: IPR 001270: IPR018368: IPR003593: IPR013461; KEGG: dak:DaAHT2_2492 ATP-dependent Clp protease, ATP-binding subunit ClpA; PFAM: ATPase AAA-2 domain protein; AAA ATPase central domain protein; Clp domain protein; Clp ATPase-like; SMART: AAA ATPase; SPTR: ATP-dependent Clp protease, ATP-binding subunit clpA; TIGRFAM: ATP-dependent Clp protease, ATP-binding subunit clpA; PFAM: AAA domain (Cdc48 subfamily); Clp amino termi [...]
  
 
 0.879
ADW17097.1
GrpE protein; COGs: COG0576 Molecular chaperone GrpE (heat shock protein); InterPro IPR000740; KEGG: dak:DaAHT2_0057 GrpE protein; PFAM: GrpE protein; SPTR: Protein grpE; PFAM: GrpE.
   
 
 0.871
Your Current Organism:
Desulfobulbus propionicus
NCBI taxonomy Id: 577650
Other names: D. propionicus DSM 2032, Desulfobulbus propionicus DSM 2032, Desulfobulbus propionicus str. DSM 2032, Desulfobulbus propionicus strain DSM 2032
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