The domain within your query sequence starts at position 63 and ends at position 244; the E-value for the CLP_protease domain shown below is 8.8e-82.



PFAM accession number:PF00574
Interpro abstract (IPR023562):

This entry includes peptidases from the MEROPS peptidase family S14, including ClpP endopeptidase and translocation-enhancing protein TepA.

ClpP is an ATP-dependent protease that cleaves a number of proteins, such as casein and albumin [ (PUBMED: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 [ (PUBMED: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.

Translocation-enhancing protein TepA displays sequence similarity to ClpP. It is required for efficient translocation of pre-proteins across the membrane [ (PUBMED:10455123) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry CLP_protease