Catalyzes the removal of dipeptides from the N-terminus of oligopeptides (PubMed:11096098, PubMed:23246913). Shows a broad specificity for both aliphatic and aromatic residues in the P1 position, with glycine or proline being not acceptable in this position (PubMed:11096098). Most potently cleaves the synthetic substrate Met-Leu-methylcoumaryl-7-amide (Met-Leu-MCA), Leu-Arg-MCA and Lys-Ala-MCA to a lesser extent (PubMed:23246913). Is likely involved in amino acid metabolism and bacterial growth of asaccharolytic P.gingivalis, that utilizes amino acids from extracellular proteinaceous nutrients as energy and carbon sources (PubMed:11096098). Is inhibited in vitro by typical serine protease inhibitors like diisopropyl fluorophosphate, Pefablock, and 3,4-dichloroisocoumarin, but not by typical cysteine class inhibitors such as E-64 or iododoacetic acid. Is active against Ala-Phe-pNA over a broad pH range, from neutral to basic pH (6.5-9.0). Optimum temperature is 43 degrees Celsius, using Ala-Phe-pNA as substrate. Belongs to the peptidase S46 family.