Involved in the inhibition of insect antibacterial peptides. Reduces the antibacterial activity of G.mellonella hemolymph by 50%. Reduces the antibacterial activity of cecropin A by 80% and cecropin B by 75%. Preferential cleavage of bonds with hydrophobic residues in P1'. Binds 1 zinc ion per subunit. Inhibited by 8 mM 1,10-phenanthroline and 10 mM EDTA, but not by PMSF. Optimum pH is 9.0. Optimum temperature is 50 degrees Celsius. Active from 10 to 80 degrees Celsius. Belongs to the peptidase M10B family.