| Type: | Domain | Name: | Peptidase A26 |
| Description: | This entry represents a transmembrane domain with a (10,12) beta-barrel structure found in a number of peptidases, which include the outer membrane protease omptin.Members of this entry belong to the MEROPS peptidase family A26 (omptin, clan AF). The omptin family, comprises a number of novel outer membrane-associated serine proteases that are distinct from trypsin-like proteases in that they cleave polypeptides between two basically-charged amino acids []. The enzyme is sensitive to the serine protease inhibitor diisopropylfluoro-phosphate, to divalent cations such as copper, zinc and iron [], and istemperature regulated, activity decreasing at lower temperatures [, ]. Temperature regulation is most prominently shown in the Yersinia pestiscoagulase/fibrinolysin protein, where coagulase activity is prevalent below 30 degrees Celsius, and fibrinolysin (protease) activity is prevalentabove this point, the optimum temperature being 37 degrees []. It is possible that this assists in 'flea blockage' and transmission of the bacteria to animals []. | Short Name: | Peptidase_A26 |
