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 and heat shock protein 70; Acts as a chaperone; Belongs to the heat shock protein 70 family. (622 aa)    
Predicted Functional Partners:
htpG
Heat shock protein HtpG, chaperone Hsp90; Molecular chaperone. Has ATPase activity.
   
 0.999
grpE
Co-chaperone protein 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 AT [...]
 
 0.999
dnaJ
Co-chaperone and heat shock protein; 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 be [...]
 0.998
cbpA
Co-chaperone-curved DNA binding protein A; Pfam matches to PF00226.22 DnaJ, and to PF01556.9 DnaJ_C.
 0.996
groEL
60 kD chaperonin (cpn60); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.993
clpB
Protein disaggregating chaperone ClpB; Pfam matches to PF02861.11 Clp_N, and to PF00004.20 AAA; Belongs to the ClpA/ClpB family.
  
 
 0.984
hrcA
Heat-inducible transcription repressor.
  
  
 0.981
groES
10 kD chaperonin (cpn10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.973
iscU
NifU-like protein; May be involved in the formation or repair of [Fe-S] clusters present in iron-sulfur proteins.
  
 
 0.966
clpA
ATP-dependent ClpAP protease, ATP-binding subunit ClpA; Pfam matches to PF00004.20 AAA, and to PF07724.5 AAA_2; Belongs to the ClpA/ClpB family.
  
 
 0.965
Your Current Organism:
Campylobacter lari
NCBI taxonomy Id: 306263
Other names: C. lari RM2100, Campylobacter lari RM2100, Campylobacter lari str. RM2100, Campylobacter lari strain RM2100
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.