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
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Coexpression
Experiments
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[Homology]
Score
hslSHeat shock protein; Associates with aggregated proteins, together with IbpA, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent. (154 aa)    
Predicted Functional Partners:
hslT
Heat shock protein; Associates with aggregated proteins, together with IbpB, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent.
 
  
0.924
clpB-2
Clp ATPase; 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 family.
  
 
 0.804
clpB
Putative Clp ATPase; Similar to Escherichia coli ClpB protein, which is thought to form part of a multi-chaperone system supressing protein aggregation, SW:CLPB_ECOLI (P03815) (857 aa) fasta scores: E(): 0, 35.1% identity in 883 aa overlap. Also similar to Yersinia enterocolitica Clp protease-associated protein ClpB TR:AAG00524 (EMBL:AF285784) (890 aa) fasta scores: E(): 0, 44.2% id in 866 aa. Contains small internal deletions relative to orthologues; Belongs to the ClpA/ClpB family.
  
 
 0.781
hslV
Heat shock protein; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
   
  
 0.762
htpG
Heat shock protein HtpG; Molecular chaperone. Has ATPase activity.
  
 
 0.760
clpA
Similar to Escherichia coli ATP-dependent Clp protease ATP-binding subunit ClpA SW:CLPA_ECOLI (P15716) (758 aa) fasta scores: E(): 0, 89.432% id in 757 aa, and to Vibrio cholerae ATP-dependent Clp protease, ATP-binding subunit ClpA TR:Q9KSW2 (EMBL:AE004194) (756 aa) fasta scores: E(): 3.8e-209, 77.303% id in 749 aa; Belongs to the ClpA/ClpB family.
  
 
 0.744
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
 
 0.740
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 [...]
  
 
 0.740
clpB5
Clp ATPase; Similar to Escherichia coli ClpB protein, which is thought to form part of a multi-chaperone system supressing protein aggregation, SW:CLPB_ECOLI (P03815) (857 aa) fasta scores: E(): 0, 37.4% identity in 866 aa overlap and to Yersinia enterocolitica Clp protease-associated protein ClpB TR:AAG00524 (EMBL:AF285784) (890 aa) fasta scores: E(): 0, 87.7% id in 884 aa. Also significantly similar to the products of the Y. pestis CDS: YPO0506, YPO0971,YPO1471, YPO3275 and YPO3599; Belongs to the ClpA/ClpB family.
  
 
 0.725
hslU
ATP-binding heat shock protein; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
   
  
 0.724
Your Current Organism:
Yersinia pestis
NCBI taxonomy Id: 214092
Other names: Y. pestis CO92, Yersinia pestis CO92, Yersinia pestis str. CO92, Yersinia pestis strain CO92
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