In molecular biology, theCLP protease family is a family ofserine peptidases belong to theMEROPS peptidase family S14 (ClpPendopeptidase family, clan SK). ClpP is anATP-dependentprotease that cleaves a number ofproteins, such ascasein andalbumin.[1] It exists as aheterodimer of ATP-binding regulatory A and catalytic P subunits, both of which are required for effective levels of protease activity in the presence of ATP,[1] although the P subunit alone does possess some catalytic activity.
Proteases highly similar to ClpP have been found to be encoded in the genome ofbacteria, in themitochondria ofmetazoa, someviruses and in thechloroplast ofplants. A number of theproteins in this family are classified as non-peptidasehomologues as they have been found experimentally to be without peptidase activity, or lackamino acid residues that are believed to be essential for catalytic activity.
Mutations in mitochondrial CLPP are associated withPerrault syndrome[2][3][4][5] and cause a variety of molecular defects, from the loss of ATPase docking, to the activation or inhibition of peptidase activity.[3][6]
^Newman, W. G.; Friedman, T. B.; Conway, G. S.; Demain LAM; Adam, M. P.; Ardinger, H. H.; Pagon, R. A.; Wallace, S. E.; Bean LJH; Stephens, K.; Amemiya, A. (1993). Adam, Margaret P.; Ardinger, Holly H.; Pagon, Roberta A.; Wallace, Stephanie E. (eds.)."Perrault Syndrome".GeneReviews. Seattle (WA): University of Washington, Seattle.PMID25254289. Retrieved2020-11-18.
^Ahmed S, Jelani M, Alrayes N, Mohamoud HS, Almramhi MM, Anshasi W, et al. (June 2015). "Exome analysis identified a novel missense mutation in the CLPP gene in a consanguineous Saudi family expanding the clinical spectrum of Perrault Syndrome type-3".Journal of the Neurological Sciences.353 (1–2):149–54.doi:10.1016/j.jns.2015.04.038.PMID25956234.S2CID6053528.
