IPR018215
ClpP, Ser active site
InterPro entry
Short name | ClpP_Ser_AS |
Description
Clp is an ATP-dependent protease that cleaves a number of proteins, such as casein and albumin
[1]. 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
[1], 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.
References
1.Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli. Maurizi MR, Clark WP, Katayama Y, Rudikoff S, Pumphrey J, Bowers B, Gottesman S. J. Biol. Chem. 265, 12536-45, (1990). View articlePMID: 2197275
Cross References
ENZYME
Contributing Member Database Entry
- PROSITE patterns:PS00381