In the food vacuole, acts downstream of proteases plasmepsins PMI and PMII and falcipains during the catabolism of host hemoglobin by cleaving peptide fragments of alpha and beta hemoglobin subunits generated by PMI and PMII and falcipains (PubMed:17074076). In the apicoplast, degrades apicoplast transit peptides after their cleavage (PubMed:17074076). Prefers bulky hydrophobic amino acids in the P1' position at both acidic and neutral pH (By similarity). At P2', prefers hydrophobic residues at acidic pH; at neutral pH, these same residues are abundant but prefers Arg (By similarity). At P3', prefers hydrophobic residues, especially Met, at both pH conditions. At P4' and P5', prefers acidic residues at acidic pH, however, at neutral pH, the enzyme is less selective at these positions (By similarity). The optimal site cleavage at acidic pH is YNEHS-|-FFMEE and, at neutral pH, MKRHS-|-FRMRG (By similarity). Binds 1 zinc ion per subunit. Monomer. Localizes to the food (or digestive) vacuole, an acidic vacuole where host hemoglobin is digested (PubMed:17074076). During the trophozoite and early to mid-schizont stages, localizes to the apicoplast (PubMed:17074076). Expressed during the asexual blood stage; expression begins at the late ring, early trophozoite stage, increases in the mid-trophozoite stage, and persists throughout the schizont stage (at protein level). Does not require processing for targeting to the food vacuole or maturation. Belongs to the peptidase M16 family.