Clp protease family
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.
| CLP_protease | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of the clpp protease catalytic domain from plasmodium falciparum | |||||||||
| Identifiers | |||||||||
| Symbol | CLP_protease | ||||||||
| Pfam | PF00574 | ||||||||
| Pfam clan | CL0127 | ||||||||
| InterPro | IPR001907 | ||||||||
| PROSITE | PDOC00358 | ||||||||
| MEROPS | S14 | ||||||||
| SCOPe | 1tyf / SUPFAM | ||||||||
| CDD | cd00394 | ||||||||
| |||||||||
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.
References
- 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.