Clp protease proteolytic subunit /Translocation-enhancing protein TepA (IPR023562)

Short name: ClpP/TepA

Overlapping homologous superfamilies

Family relationships


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 [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.

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

Contributing signatures

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