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
groELClass I heat-shock protein (chaperonin); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. (544 aa)    
Predicted Functional Partners:
groES
Class I heat-shock protein (chaperonin); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family.
 
 
 0.999
dnaK
Class I heat-shock protein (chaperonin); Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.994
grpE
Heat-shock protein (activation of DnaK); 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. Severa [...]
 
 0.985
dnaJ
Heat-shock protein (activation of DnaK); 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 interaction [...]
 
 0.956
htpG
Class III heat-shock protein (chaperonin); Molecular chaperone. Has ATPase activity.
   
 
 0.927
fliY
Flagellar motor switch protein; FliN is one of three proteins (FliG, FliN, FliM) that form the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. Belongs to the FliN/MopA/SpaO family.
   
 
 0.906
hrcA
Transcriptional repressor of class I heat-shock genes; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons.
  
  
 0.888
clpY
ATP-dependent Clp protease (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.
   
  
 0.855
lonA
ATP-dependent proteinase La 1 (lon) (class III heat-shock protein); ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
  
 0.795
clpQ
Beta-type subunit of the 20S proteasome; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
   
 
 0.777
Your Current Organism:
Bacillus halodurans
NCBI taxonomy Id: 272558
Other names: B. halodurans C-125, Bacillus halodurans C-125, Bacillus halodurans str. C-125, Bacillus halodurans strain C-125
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