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slr0195 slr0195 slr1767 slr1767 ssr2962 ssr2962 clpB1 clpB1 clpP3 clpP3 clpR clpR clpC clpC clpX clpX uvrB uvrB clpB2 clpB2 uvrA uvrA
"clpR" - ATP-dependent Clp protease proteolytic subunit in Synechocystis sp. PCC6803
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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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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[Homology]
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clpRATP-dependent Clp protease proteolytic subunit; Has lost the two conserved residues (Ser and His) proposed to be part of the active site. Therefore it could be inactive (225 aa)    
Predicted Functional Partners:
clpX
ATP-dependent protease ATPase subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (445 aa)
 
  0.990
clpB1
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) (898 aa)
   
 
  0.960
clpB2
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) (872 aa)
   
 
  0.960
clpC
ATP-dependent Clp protease regulatory subunit (821 aa)
   
 
  0.935
uvrA
Excinuclease ABC subunit A; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate (970 aa)
     
 
  0.759
slr0195
Hypothetical protein (183 aa)
           
  0.753
slr1767
Hypothetical protein (112 aa)
           
  0.753
ssr2962
Hypothetical protein (74 aa)
           
  0.753
uvrB
Excinuclease ABC subunit B; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate [...] (669 aa)
       
 
  0.750
clpP3
ATP-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 (202 aa)
 
     
0.744
Your Current Organism:
Synechocystis sp. PCC6803
NCBI taxonomy Id: 1148
Other names: Aphanocapsa sp. (strain N-1), Aphanocapsa sp. N-1, S. sp. PCC 6803, Synechocystis, Synechocystis PCC6803, Synechocystis sp. (ATCC 27184), Synechocystis sp. (PCC 6803), Synechocystis sp. (strain PCC 6803), Synechocystis sp. ATCC 27184, Synechocystis sp. PCC 6803, Synechocystis sp. PCC 6803 A, Synechocystis sp. PCC 6803 B, Synechocystis sp. PCC6803
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