AC MF_00698; DC Protein; auto TR HAMAP; MF_00698; -; 1; level=0 XX Names: Aminopeptidase_S15 XX ID PEPX DE RecName: Full=Xaa-Pro dipeptidyl-peptidase; DE EC=3.4.14.11; DE AltName: Full=X-Pro dipeptidyl-peptidase; DE AltName: Full=X-prolyl-dipeptidyl aminopeptidase; DE Short=X-PDAP; GN Name=pepX; XX CC -!- FUNCTION: Removes N-terminal dipeptides sequentially from polypeptides CC having unsubstituted N-termini provided that the penultimate residue is CC proline. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolyzes Xaa-Pro-|- bonds to release unblocked, N-terminal CC dipeptides from substrates including Ala-Pro-|-p-nitroanilide and CC (sequentially) Tyr-Pro-|-Phe-Pro-|-Gly-Pro-|-Ile.; EC=3.4.14.11; CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the peptidase S15 family. XX DR Pfam; PF02129; Peptidase_S15; 1; trigger=no DR PRINTS; PR00923; LACTOPTASE; 1; trigger=no XX KW Cytoplasm KW Hydrolase KW Protease KW Serine protease KW Aminopeptidase XX GO GO:0008239; F:dipeptidyl-peptidase activity GO GO:0005737; C:cytoplasm XX FT From: PEPX_LACLC (P22346) FT ACT_SITE 348 FT /note="Charge relay system" FT Condition: S FT ACT_SITE 468 FT /note="Charge relay system" FT Condition: D FT ACT_SITE 498 FT /note="Charge relay system" FT Condition: H XX Size: 755-813; Related: None; Template: P22346; Q93M42; Scope: Bacteria; Lactobacillales Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.18 2019/11/18 //