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. (647 aa)    
Predicted Functional Partners:
grpE
Co-chaperone GrpE; 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-depend [...]
 
 
 0.995
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 [...]
 0.987
htpG
Chaperone protein HtpG; Molecular chaperone. Has ATPase activity.
  
 0.983
AEF84968.1
Peptidyl-prolyl cis-trans isomerase; Identified by match to protein family HMM PF00160; match to protein family HMM PF00254.
 0.955
AEF84143.1
Molecular chaperone, DnaJ family; Identified by match to protein family HMM PF00226.
 
 0.938
groL
Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 
 0.928
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.
  
 
 0.915
AEF85238.1
Chaperone protein DnaK; Identified by match to protein family HMM PF00012; Belongs to the heat shock protein 70 family.
  
  
 
0.904
AEF84723.1
Tetratricopeptide repeat protein; Identified by match to protein family HMM PF00515; match to protein family HMM PF07719.
 
 0.894
AEF84598.1
IscU protein; Identified by match to protein family HMM PF01592; match to protein family HMM PF04324.
  
 
 0.893
Your Current Organism:
Treponema primitia ZAS2
NCBI taxonomy Id: 545694
Other names: T. primitia ZAS-2, Treponema primitia ZAS-2, Treponema primitia str. ZAS-2, Treponema primitia strain ZAS-2, Treponema sp. ZAS-2
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.