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Preferentially cleaves the peptide bond following two basic residues, one of which is Lys, but does not recognize the bond following a single basic residue (PubMed:16487335). Probable potent virulence factor that cleaves various host plasma proteins, including prekallikrein, prothrombin and fibrinogen (PubMed:16487335, PubMed:17142774, PubMed:18067862, PubMed:18462393, PubMed:19654332). ASP induces vascular leakage and reduction in blood pressure by activating the host plasma kallikrein/kinin system (PubMed:12153115, PubMed:16487335, PubMed:17142774). It affects the host coagulation system during infection through activation of prothrombin to alpha-thrombin and degradation of fibrinogen, which impairs plasma clottability (PubMed:18067862, PubMed:18462393). It also hydrolyzes the complement component C5, releasing the C5a anaphylatoxin, which causes the formation of pus and edema (PubMed:18714034). In addition, degrades its external chaperone ORF2 after the secretion of the ASP-ORF2 complex (PubMed:25784551)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Cleavage of -Lys-Lys-|-Xaa and -Lys-Arg-|-Xaa bonds.","ecNumber":"3.4.21.121","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16487335"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18067862"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18462393"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19654332"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Ca(2+)","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19654332"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"25784551"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29108"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19654332"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25784551"}],"value":"Binds 3 calcium ions per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11092244"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12153115"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12446656"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23089609"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25784551"}],"value":"Folding, maturation and production of the active form of the protease by the cell requires a protein (ORF2), encoded just downstream of asp, which acts as a chaperone (PubMed:11092244, PubMed:12446656, PubMed:25784551). Formation of a complex with ORF2 in the periplasm also inactivates the protease activity and likely protects ASP from intrinsic proteases (PubMed:25784551). In vitro, protease activity is inhibited by human alpha-2-macroglobulin, suggesting that this inhibitor can impede ASP virulence activities in A.sobria infection sites (PubMed:23089609). However, slow ASP inhibition by alpha-2-macroglobulin in plasma may indicate insufficient ASP control in vivo (PubMed:23089609). Activity is inhibited by serine protease inhibitors such as 4-(2-aminoethyl)-benzenesulfonyl fluoride (AEBSF) and diisopropyl fluorophosphate (DFP) (PubMed:11092244, PubMed:12153115). Not inhibited by metallo-protease inhibitors and cysteine protease inhibitors (PubMed:12153115). The treatment with reagents to modify sulfhydryl group do not reduce the activity (PubMed:12153115)"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12153115"}],"value":"Optimum pH is 7.5."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12446656"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25784551"}],"value":"Forms a complex with the chaperone ORF2 in the periplasm (PubMed:12446656, PubMed:25784551). 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