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CLPP5 protein (Arabidopsis thaliana) - STRING interaction network
"CLPP5" - Nuclear encoded CLP protease 5 in Arabidopsis thaliana
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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:
some 3D structure is known or predicted
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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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CLPP5Nuclear encoded CLP protease 5; 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 (By similarity) (298 aa)    
Predicted Functional Partners:
CLPP3
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 (By similarity). In the absence of CLPP3, modified ClpPR core(s) could be formed, albeit at strongly reduced levels (PubMed-23548781) (309 aa)
   
0.986
CLPX
CLP protease regulatory subunit X; ATP-dependent specificity component of the mitochondrial Clp protease (PubMed-11352464). It directs the protease to specific substrates (By similarity). Can perform chaperone functions in the absence of ClpP (By similarity) (579 aa)
 
 
  0.984
AT5G49840
ATP-dependent Clp protease; ATP-dependent specificity component of the mitochondrial Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (608 aa)
 
 
  0.982
AT4G25370
Double Clp-N motif protein; Accessory protein regulating the assembly of the plastidial Clp protease system (PubMed-21266658, PubMed-25921872). CLPT1 first binds to the heptameric P-ring containing the CLP3-6 subunits followed by CLPT2, and only then does the P-ring combine with the R-ring composed of the clpP1 and CLPR1-4 subunits (PubMed-21266658). Once the core complex is fully assembled, it then associates to the CLPC chaperone partner to form the functional protease (PubMed-21266658). CLPT1 and CLPT2 are partially redundant (PubMed-25921872) (238 aa)
   
 
  0.979
CLP2
CLP protease proteolytic subunit 2; Required for chloroplast development and integrity. Involved in the regulation of plastoglobules formation (279 aa)
   
 
0.960
CLPR1
CLP protease proteolytic subunit 1; Required for chloroplast development and differentiation (387 aa)
   
 
0.958
CLPP4
CLP protease P4; 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 (By similarity). Essential protein required for chloroplast development and integrity (PubMed-16705403, PubMed-17241447). Essential for Embryogenesis (PubMed-23548781) (292 aa)
   
 
0.951
AT1G33360
ATP-dependent Clp protease; ATP-dependent specificity component of the mitochondrial Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (656 aa)
 
 
  0.948
AT4G12060
Double Clp-N motif protein; Accessory protein regulating the assembly of the plastidial Clp protease system (PubMed-21266658, PubMed-25921872). CLPT1 first binds to the heptameric P-ring containing the CLP3-6 subunits followed by CLPT2, and only then does the P-ring combine with the R-ring composed of the clpP1 and CLPR1-4 subunits (PubMed-21266658). Once the core complex is fully assembled, it then associates to the CLPC chaperone partner to form the functional protease (PubMed-21266658). CLPT2 and CLPT1 are partially redundant (PubMed-25921872) (241 aa)
     
 
  0.946
CLPC1
CLPC homologue 1; Molecular chaperone that hydrolyzes ATP and is associated with the chloroplast protein import apparatus. May function as the motor for chloroplast protein translocation, as translocation requires ATP hydrolysis in the stroma. May interact with a ClpP-like protease involved in degradation of denatured proteins in the chloroplast. Involved in the regulation of chlorophyll b biosynthesis through the destabilization of chlorophyllide a oxygenase (CAO) protein in response to the accumulation of chlorophyll b. Involved in leaf iron homeostasis (929 aa)
   
 
  0.910
Your Current Organism:
Arabidopsis thaliana
NCBI taxonomy Id: 3702
Other names: A. thaliana, Arabidopsis thaliana, Arabidopsis thaliana (L.) Heynh., mouse-ear cress, thale cress, thale-cress
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