InterPro : IPR004236

Name  Peptidase S1A, alpha-lytic prodomain Short Name  Pept_S1_alpha_lytic
Type  Domain Description  Proteolytic enzymes that exploit serine in their catalytic activity are ubiquitous, being found in viruses, bacteria and eukaryotes []. They include a wide range of peptidase activity, including exopeptidase, endopeptidase, oligopeptidase and omega-peptidase activity. Many families of serine protease have been identified, these being grouped into clans on the basis of structural similarity and other functional evidence []. Structures are known for members of the clans and the structures indicate that some appear to be totally unrelated, suggesting different evolutionary origins for the serine peptidases [].Not withstanding their different evolutionary origins, there are similarities in the reaction mechanisms of several peptidases. Chymotrypsin, subtilisin and carboxypeptidase C have a catalytic triad of serine, aspartate and histidine in common: serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base []. The geometric orientations of the catalytic residues are similar between families, despite different protein folds []. The linear arrangements of the catalytic residues commonly reflect clan relationships. For example the catalytic triad in the chymotrypsin clan (PA) is ordered HDS, but is ordered DHS in the subtilisin clan (SB) and SDH in the carboxypeptidase clan (SC) [, ].The alpha-lytic protease prodomain is associated with serine peptidases, specifically the alpha-lytic endopeptidases and streptogrisin A, B, C, D and E, which are bacterial enzymes and which belong to MEROPS peptidase subfamily S1A (). The protease precursor in Gram-negative bacterial proteases may be a general property of extracellular bacterial proteases []. The proteases are encodedwith a large (166 amino acid) N-terminal pro region that is required transiently both in vivoand in vitrofor the correct folding of the protease domain [, ]. The pro region also acts as a potent inhibitor of the mature enzyme [].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

0 Contains

1 Found In

Id Name Short Name Type
IPR001316 Peptidase S1A, streptogrisin Pept_S1A_streptogrisin Family

0 Parent Features

6 Publications

First Author Title Year Journal Volume Pages
Rawlings ND Evolutionary families of peptidases. 1993 Biochem J 290 ( Pt 1) 205-18
Rawlings ND Families of serine peptidases. 1994 Methods Enzymol 244 19-61
Silen JL Molecular analysis of the gene encoding alpha-lytic protease: evidence for a preproenzyme. 1988 Gene 69 237-44
Silen JL The alpha-lytic protease pro-region does not require a physical linkage to activate the protease domain in vivo. 1989 Nature 341 462-4
Baker D A protein-folding reaction under kinetic control. 1992 Nature 356 263-5
Baker D Protease pro region required for folding is a potent inhibitor of the mature enzyme. 1992 Proteins 12 339-44

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)