Dominant secreted aspartyl protease that has a clear preference for aromatic residues in the P1' position directly adjacent to the cleavage site and, in particular, Trp. In addition, it generally cleaves peptides containing Lys, Arg, Phe, Tyr, or Nle (norleucine) in the P1 position, Nle and Glu at P2, and Arg and Val at P2'. Has important roles in facilitating the interaction of the yeast with the external environment (PubMed:29246799). Is able to rapidly hydrolyze Staphylococcus aureus protein A, an important S.aureus virulence factor involved in immune evasion and biofilm formation. Shows anti-biofilm properties and thus plays a role in inter-kingdom interactions, beneficial for host skin health (PubMed:29246799). Inhibited by pepstatin A. Highly expressed during exponential growth in rich media (PubMed:29246799). Also part of the 3 most highly expressed extracellular proteases in minimal media (PubMed:29246799). Expressed on human skin (PubMed:29246799). Belongs to the peptidase A1 family.