| Type: | Active_site | Name: | ClpP, active site |
| 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 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.The ClpP active sites represented by this entry are based around two of the residues involved in the catalytic triad (a serine and a histidine) and are highly conserved. | Short Name: | ClpP_AS |
