Degrades abnormal exported proteins and responsible for the propeptide processing of a natural pro-protein and for the maturation of a native protein. It also plays a prominent role in stress (heat shock, ethanol, puromycin and NaCl) resistance during active exponential growth (By similarity). Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val. Inactivation leads to reduce the efficiency of secretion of the recombinant protein produced, although the protein produced is completely stabilized. Belongs to the peptidase S1C family.