STRINGSTRING
clpP clpP clpX clpX clpA clpA groEL groEL groES groES dnaK dnaK clpB clpB lon lon clpS clpS hslU hslU lon-2 lon-2
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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clpPATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. (213 aa)    
Predicted Functional Partners:
clpX
ATP-dependent Clp protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
 
 0.999
clpA
ATP-binding protease component ClpA; Product name confidence: Class 2 (High similarity to functionally studied protein); Belongs to the ClpA/ClpB family.
   
 
 0.977
groEL
GroEL protein; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 
 0.959
groES
GroES protein; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 
 0.948
dnaK
DnaK protein; Acts as a chaperone; Belongs to the heat shock protein 70 family.
   
 
 0.939
clpB
ClpB protein; 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.
  
 
 0.938
lon
Lon protease; 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.
  
 
 0.932
clpS
Conserved hypothetical protein; Involved in the modulation of the specificity of the ClpAP- mediated ATP-dependent protein degradation; Belongs to the ClpS family.
   
 
 0.914
hslU
Heat shock protein HslU; 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.
 
  
 0.904
lon-2
Probable ATP-dependent protease; 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.
  
 
 0.900
Your Current Organism:
Pseudomonas aeruginosa
NCBI taxonomy Id: 208964
Other names: P. aeruginosa PAO1, Pseudomonas aeruginosa PAO1, Pseudomonas sp. PAO1
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