PrcA catalytic domain (IPR034054)

Short name: Pep_S8_PrcA

Overlapping homologous superfamilies

Domain relationships


This entry includes the peptidase domain of the bacterial members of peptidase subfamily S8B, which also includes dibasic processing peptidases from eukaryotes. The characterized bacterial peptidases have a trypsin-like specificity, cleaving lysyl or arginyl bonds. PrcA peptidase (MEROPS identifier S08.079) is a calcium-dependent peptidase isolated from Anabaena located in the cytoplasm and synthesized as a precursor [PMID: 8944762]. The HreP peptidase from Yersinia enterocolitica (MEROPS identifier S08.043) is also synthesized with a propeptide and processes itself by cleavage of a lysyl bond [PMID: 11371518]. It is essential for virulence and the hreP gene is regulated by three genes, pypA, pypB and pypC [PMID: 19114497].

Peptidases S8 (or subtilases serine endo- and exo-peptidase clan) have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values [PMID: 1798697, PMID: 8420571, PMID: 8439290, PMID: 9070434].

Contributing signatures

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