STRINGSTRING
dnaK dnaK grpE grpE dnaJ dnaJ htpG htpG ACS79636.1 ACS79636.1 ACS78205.1 ACS78205.1 ACS79373.1 ACS79373.1 ACS78491.1 ACS78491.1 ACS79892.1 ACS79892.1 ACS79440.1 ACS79440.1 clpB clpB
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.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
dnaKChaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (638 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 [...]
 
 0.999
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 [...]
 0.998
htpG
Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity.
  
 0.998
ACS79636.1
PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; KEGG: dvl:Dvul_1288 chaperone DnaJ domain-containing protein.
 0.995
ACS78205.1
Fe-S cluster assembly protein NifU; May be involved in the formation or repair of [Fe-S] clusters present in iron-sulfur proteins.
  
 
 0.974
ACS79373.1
PFAM: heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; KEGG: dde:Dde_1302 heat shock protein DnaJ-like.
 
 0.972
ACS78491.1
KEGG: gme:Gmet_3315 AAA ATPase; TIGRFAM: type VI secretion ATPase, ClpV1 family; PFAM: ATPase AAA-2 domain protein; AAA ATPase central domain protein; ATPase associated with various cellular activities AAA_5; SMART: AAA ATPase; Belongs to the ClpA/ClpB family.
 
 
 0.970
ACS79892.1
KEGG: dde:Dde_2099 ATPase; TIGRFAM: ATP-dependent Clp protease, ATP-binding subunit clpA; PFAM: ATPase AAA-2 domain protein; AAA ATPase central domain protein; Torsin; ATPase associated with various cellular activities AAA_5; Clp domain protein; SMART: AAA ATPase; Belongs to the ClpA/ClpB family.
 
 
 0.970
ACS79440.1
PFAM: cytochrome c class III; KEGG: dvl:Dvul_2405 cytochrome c, class III.
  
 0.968
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.
  
 
 0.966
Your Current Organism:
Desulfovibrio salexigens
NCBI taxonomy Id: 526222
Other names: D. salexigens DSM 2638, Desulfovibrio salexigens ATCC 14822, Desulfovibrio salexigens DSM 2638, Desulfovibrio salexigens str. DSM 2638, Desulfovibrio salexigens strain DSM 2638
Server load: low (26%) [HD]