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https://bar.utoronto.ca/thalemine/service/ is incorrect| Description | This entry includes autotransporter serine proteases belonging to the peptidase S8 (subtilase). Autotransporters are outer membrane/secreted proteins of Gram-negative bacteria. The presence of these subtilisin-like domains in these autotransporters may enable them to be auto-catalytic and may also serve to allow them to act as a maturation protease cleaving other outer membrane proteins at the cell surface. Included in this entry are: the SphB1 peptidase from Bordetella pertussis, the causative agent of whooping cough, which is required for the maturation of filamentous hemagglutinin adhesin at the bacterial surface (FHA) [ ]; an extracellular subtilisin SSP from Serratia (MEROPS identifier S08.094), which has a large C-terminal domain that forms a pore in the outer membrane through which the mature enzyme can pass []; and the AasP peptidase from Actinobacillus pleuropneumoniae (MEROPS identifier S08.144), the causative agent of porcine pleuropneumonia, which does not undergo autoproteolysis, but is still an active sheddase, releasing fragments of the OmlA protein [].This domain is part of a family of domains found in serine peptidases belonging to the MEROPS peptidase families S8 (subfamilies S8A (subtilisin) and S8B (kexin)) and S53 (sedolisin), both of which are members of clan SB [ , , , ].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 [ , , , ]. | Name | Autotransporter serine protease peptidase domain |
| Short Name | Peptidases_S8_Autotransporter | Type | Domain |
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