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
dnaKMolecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. (641 aa)    
Predicted Functional Partners:
dnaJ
Molecular chaperone; 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, DnaK [...]
 0.999
grpE
Putative GrpE chaperone; 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- [...]
 
 0.999
htpG
tRNA-Leu; Molecular chaperone. Has ATPase activity.
  
 0.992
cbpA
Similar to Escherichia coli curved DNA-binding protein CbpA or B1000 SW:CBPA_ECOLI (P36659) (306 aa) fasta scores: E(): 2.9e-26, 41.772% id in 316 aa, and to Caulobacter crescentus DnaJ family protein cc2772 TR:Q9A4Q8 (EMBL:AE005942) (314 aa) fasta scores: E(): 4.2e-31, 41.742% id in 333 aa.
 
 0.992
clpB
ATP-dependent protease, ATPase subunit; 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to the ClpA/ClpB [...]
  
 
 0.987
cpn60
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.963
cpn10
10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 
 0.950
clpA
Similar to Escherichia coli ATP-dependent Clp protease ATP-binding subunit ClpA or LopD or B0882 or Z1119 or Ecs0968 SW:CLPA_ECOLI (P15716) (758 aa) fasta scores: E(): 8.5e-171, 61.73% id in 763 aa. Also similar to BP1198, 37.133% identity (46.014% ungapped) in 886 aa overlap; Belongs to the ClpA/ClpB family.
 
 
 0.932
hrcA
Heat-inducible transcription repressor; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons.
  
  
 0.912
iscU
[Fe-S] cluster formation/repair protein; A scaffold on which IscS assembles Fe-S clusters. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters.
  
 
 0.873
Your Current Organism:
Bordetella pertussis
NCBI taxonomy Id: 257313
Other names: B. pertussis Tohama I, Bordetella pertussis Tohama I
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