Summary for clan PE

Summary Alignment Structure Literature
HistoryMEROPS 9.8 (17 December 2012)
DescriptionSerine or threonine nucleophile; N-terminal nucleophile
Contents of clanClan PE contains self-processing peptidases.
EvidenceThe protein fold of the type peptidase of the clan is not closely similar to those of peptidases in any other clan. Clan PE contains peptidases of mixed catalytic type, in which the nucleophile can be either serine or threonine.
Catalytic mechanismThe peptidase DmpA (P01.001) is an N-terminal nucleophile hydrolase, but is not homologous to those in clan PB (Fanuel et al., 1999). (See also family P1.)
Peptidase activity(See family P1.)
Protein foldThe tertiary structure of aminopeptidase DmpA from Ochrobactrum anthropi has been determined (P01.001; Bompard-Gilles et al., 2000). Peptidases in clan PE have an internal duplication, and each repeat consists two layers, a layer of helices and a beta sheet. The catalytic serine or threonine is at the start of one of the strands in the C-terminal repeat.
Homologous non-peptidase familiesGlutamate N-acetyltransferase 2 from Streptomyces clavuligerus and molybdenum cofactor-binding domain have related structures. The fold is similar to that of the Ntn-hydrolases in clan PB, but this is believed to be a result of convergent evolution (Cheng & Grishin, 2005).


Family Family Type Peptidase Structure
P1 DmpA aminopeptidase (Ochrobactrum anthropi) Yes
T5 ornithine acetyltransferase precursor (Saccharomyces cerevisiae) Yes

Distribution of clan PE among Kingdoms of Organisms