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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dnaKChaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (641 aa)    
Predicted Functional Partners:
grpE
GrpE protein; 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 [...]
 
 0.986
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 [...]
 0.979
Psta_4209
PFAM: chaperone DnaJ domain protein; heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; KEGG: scl:sce0617 DnaJ molecular chaperone.
 0.967
Psta_3418
PFAM: heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; KEGG: dar:Daro_2024 peptidase S1C, Do.
  
 0.963
Psta_2082
2-alkenal reductase; PFAM: Heat shock protein 70; KEGG: bca:BCE_1142 DnaK protein, truncation.
  
  
 
0.918
Psta_1316
TIGRFAM: SUF system FeS assembly protein, NifU family; PFAM: nitrogen-fixing NifU domain protein; KEGG: SUF system FeS assembly protein, NifU family.
  
 0.875
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.
  
 
 0.845
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.821
Psta_1838
KEGG: pap:PSPA7_0162 type VI secretion ATPase; TIGRFAM: type VI secretion ATPase, ClpV1 family; PFAM: ATPase AAA-2 domain protein; AAA ATPase central domain protein; Clp domain protein; ATPase associated with various cellular activities AAA_5; SMART: AAA ATPase; Belongs to the ClpA/ClpB family.
  
 
 0.820
Psta_1884
PFAM: ATPase AAA-2 domain protein; AAA ATPase central domain protein; UvrB/UvrC protein; ATPase associated with various cellular activities AAA_5; Clp domain protein; SMART: AAA ATPase; KEGG: bsu:BSU00860 class III stress response- related ATPase; Belongs to the ClpA/ClpB family.
  
 
 0.820
Your Current Organism:
Pirellula staleyi
NCBI taxonomy Id: 530564
Other names: P. staleyi DSM 6068, Pirellula staleyi ATCC 27377, Pirellula staleyi DSM 6068, Pirellula staleyi str. DSM 6068, Pirellula staleyi strain DSM 6068
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