Active Site

ClpP, Ser active site (IPR018215)

Short name: ClpP_Ser_AS


Clp is an ATP-dependent protease that cleaves a number of proteins, such as casein and albumin [PMID: 2197275]. 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 [PMID: 2197275], 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.

This entry represents a conserved region containing a serine that is involved in the catalytic triad.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns