Clp protease family

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PDB 2f6i EBI.jpg
crystal structure of the clpp protease catalytic domain from plasmodium falciparum
Symbol CLP_protease
Pfam PF00574
Pfam clan CL0127
InterPro IPR001907
SCOP 1tyf
CDD cd00394

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, 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.

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  1. ^ a b Maurizi MR, Clark WP, Katayama Y, Rudikoff S, Pumphrey J, Bowers B, Gottesman S (July 1990). "Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli". J. Biol. Chem. 265 (21): 12536–45. PMID 2197275. 

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This article incorporates text from the public domain Pfam and InterPro IPR001907