Secreted metalloproteinase that allows assimilation of proteinaceous substrates and probably acts as a virulence factor (By similarity). Catalyzes the hydrolysis of elastin (PubMed:7927676, PubMed:8188335). Hydrolyzes azocasein, synthetic fluorigenic substrate Abz-Ala-Ala-Phe-Phe-pNA, and His-Leu, Ala-Leu, Tyr-Leu, Gly-Phe, and Phe-Phe peptide bonds in the B chain of insulin (PubMed:8188335). Binds 1 zinc ion per subunit. Completely inhibited by metalloprotease inhibitors EDTA, 1,10-phenanthroline, and phosphoramidon, but not by inhibitors specific for serine, cysteine, and aspartate proteases, such as PMSF, antipain, leupeptin, chymostatin, and pepstatin. Zn(2+) and, to a lesser extent, Co(2+) reversed the inhibition of 1,10-phenanthroline. Optimum pH is 7.5-8.0. Optimum temperature is 60 degrees Celsius against azocasein. Retains 50% of the activity by incubation at 60 degrees Celsius for 1 hour. Secreted in the neutropenic mouse lungs by invading Aspergillus fumigatus. By Zn(2+) (PubMed:8188335). Expression is controlled by the prtT transcription factor (PubMed:19564390, PubMed:19564385). Not glycosylated according to PubMed:8188335, but glycosylated according to PubMed:24100314. Causes an allergic reaction in human. Recombinant protein binds to IgE in 93% of the 54 patients tested suffering with allergic bronchopulmonary aspergillosis (ABPA). Recombinant protein binds to IgE in 74% of the 35 A.fumigatus-allergic patients tested without ABPA. Belongs to the peptidase M36 family.