| Type: | Family | Name: | Peptidase S1B |
| Description: | This group of serine peptidases belong to the MEROPS peptidase family S1, subfamily S1B (clan PA(S)). A type example is glutamyl endopeptidase I from Staphylococcus aureus.Other members include S. aureus V8 protease, which preferentially cleaves peptide bonds C-terminal to Asp and Glu residues; Bacillus licheniformisglutamate-specific endopeptidase [], which also cleaves on the C-terminal side of acidic residues, but with strong preference for glutamate; Bacillus subtilisextracellular 'metalloprotease' []; and S. aureus exfoliative (or epidermolytic) toxins A and B, which cause impetigous diseases (also known as Staphylococcal scalded skin syndrome).In a number of prokaryotic proteases the catalytic activity is provided by a charge relay system analogous to that of the trypsin family of serineproteases, but which probably evolved by independent convergent evolution [, ]. The sequences around the catalytic residues (Asp, Ser and His) are completely different from those of the corresponding residues in trypsin serine proteases, although these proteins also contain the serine protease trypsin family signatures. | Short Name: | Peptidase_S1B |
