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clpR protein (Synechococcus elongatus PCC7942) - STRING interaction network
"clpR" - Putative ATP-dependent Clp protease proteolytic subunit-like in Synechococcus elongatus PCC7942
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Known Interactions
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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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clpRPutative ATP-dependent Clp protease proteolytic subunit-like; Has lost the two conserved residues (Ser and His) proposed to be part of the active site. Therefore it could be inactive (228 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 (449 aa)
 
  0.954
clpP3
ATP-dependent Clp protease proteolytic subunit 3; 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 (199 aa)
 
     
0.816
clpB1
Chaperone protein ClpB 1; 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). Necessary for thermotolerance; Belongs [...] (883 aa)
     
 
  0.781
ABB58566.1
annotation not available (177 aa)
   
   
  0.781
ABB56292.1
annotation not available (824 aa)
     
 
  0.779
murB
UDP-N-acetylenolpyruvoylglucosamine reductase; Cell wall formation (301 aa)
   
     
  0.634
clpB2
Chaperone protein ClpB 2; 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) (895 aa)
     
 
  0.588
ABB57028.1
ATP-dependent zinc metalloprotease FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family (632 aa)
     
   
  0.585
ABB56972.1
ATP-dependent zinc metalloprotease FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family (630 aa)
     
   
  0.585
ABB56329.1
ATP-dependent zinc metalloprotease FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family (613 aa)
     
   
  0.585
Your Current Organism:
Synechococcus elongatus PCC7942
NCBI taxonomy Id: 1140
Other names: Anacystis nidulans R2, S. elongatus PCC 7942, Synechococcus elongatus PCC 7942, Synechococcus elongatus PCC7942, Synechococcus leopoliensis UTEX 2434, Synechococcus leopoliensis strain PCC 7942, Synechococcus sp. IAM M-200, Synechococcus sp. PCC 7942
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