STRINGSTRING
STRING protein interaction network
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. (644 aa)    
Predicted Functional Partners:
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 [...]
 0.989
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 [...]
 
 0.987
Slin_5708
PFAM: chaperone DnaJ domain protein; heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; KEGG: dde:Dde_1659 heat shock protein DnaJ-like.
 0.984
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.937
Slin_1459
ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity.
 
 
 0.930
Slin_5709
KEGG: rsh:Rsph17029_3728 HSP90 family molecular chaperone-like protein.
   
 0.930
Slin_5724
SMART: TIR protein; KEGG: pin:Ping_2692 heat shock protein 70.
  
  
 
0.927
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.
  
 
 0.867
Slin_4100
PFAM: ATPase AAA-2 domain protein; Clp ATPase-like; AAA ATPase central domain protein; ATPase associated with various cellular activities AAA_5; SMART: AAA ATPase; KEGG: oan:Oant_1039 ATPase; Belongs to the ClpA/ClpB family.
  
 
 0.838
Slin_1370
PFAM: ATPase AAA-2 domain protein; Clp ATPase-like; AAA ATPase central domain protein; UvrB/UvrC protein; ATPase associated with various cellular activities AAA_5; Clp domain protein; SMART: AAA ATPase; KEGG: hypothetical protein; K03696 ATP-dependent Clp protease ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family.
  
 
 0.833
Your Current Organism:
Spirosoma linguale
NCBI taxonomy Id: 504472
Other names: S. linguale DSM 74, Spirosoma linguale DSM 74, Spirosoma linguale str. DSM 74, Spirosoma linguale strain DSM 74
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.