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. (641 aa)    
Predicted Functional Partners:
dnaJ1
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
grpE
Probable heat shock 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 round [...]
 
 0.998
dnaJ2
Putative chaperone protein dnaJ. homology to dnaJ of E. coli of 32% (sprot|DNAJ_ECOLI) Acts as a co-chaperone. Stimulates jointly with grpE the ATPase activity of dnaK (By similarity). Pfam: DnaJ domain, DnaJ central domain (4 repeats), DnaJ Cterminal region no singal peptide no TMHs; Family membership.
 
 0.992
htpG
Probable chaperon protein HtpG; Molecular chaperone. Has ATPase activity.
  
 0.989
azo0358
Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases).
  
 0.987
azo2661
Hypothetical protein which carries at the C-terminus a DnaJ N-terminal domain. InterPro: DnaJ N-terminal domain (IPR001623) Pfam: DnaJ domain no signal peptide no TMHs.
  
 0.963
clpA
ATP-dependent Clp protease ATP-binding subunit clpA. Homology to clpA of E. coli of 63% (sprot|CLPA_ECOLI). ATP-dependent specificity component of the clpP protease. It directs the protease to specific substrates. The primary function of the clpA-clpP complex appears to be the degradation of unfolded or abnormal proteins. InterPro: AAA-protein (ATPases associated with various cellular activities)(IPR003959); AAA ATPase superfamily (IPR003593); Clp amino terminus (IPR004176); chaperonins clpA/B (IPR001270); Bacterial typeII secretion system protein E (IPR001482) Pfam: Clp amino ternimal [...]
 
 
 0.940
groEL1
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 
 0.933
groEL3
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 
 0.933
clpB1
Probable ATP-dependent Clp protease, ATP-binding subunit 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.
  
 
 0.931
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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