In molecular biology, the CLP protease family is a family of
serine peptidases belong to the
MEROPS peptidase family S14 (ClpP
endopeptidase family, clan SK). ClpP is an
ATP-dependent
protease that cleaves a number of
proteins, such as
casein and
albumin.[1] It exists as a
heterodimer 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 of
bacteria, in the
mitochondria of
metazoa, some
viruses and in the
chloroplast of
plants. A number of the
proteins in this family are classified as non-peptidase
homologues as they have been found experimentally to be without peptidase activity, or lack
amino acid residues that are believed to be essential for catalytic activity.
Mutations in mitochondrial CLPP are associated with
Perrault 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. Retrieved 2020-11-18.
^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.