| Primary Identifier | IPR018215 | Type | Active_site |
| Short Name | ClpP_Ser_AS |
| description | Clp is an ATP-dependent protease that cleaves a number of proteins, such as casein and albumin []. 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 ofATP [], although the P subunit alone does possess some catalytic activity.Proteases highly similar to ClpP have been found to be encoded in the genomeof 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. |
