ID   PEPX_STRS7              Reviewed;         761 AA.
AC   C0MEP5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Xaa-Pro dipeptidyl-peptidase {ECO:0000255|HAMAP-Rule:MF_00698};
DE            EC=3.4.14.11 {ECO:0000255|HAMAP-Rule:MF_00698};
DE   AltName: Full=X-Pro dipeptidyl-peptidase {ECO:0000255|HAMAP-Rule:MF_00698};
DE   AltName: Full=X-prolyl-dipeptidyl aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00698};
DE            Short=X-PDAP {ECO:0000255|HAMAP-Rule:MF_00698};
GN   Name=pepX {ECO:0000255|HAMAP-Rule:MF_00698}; OrderedLocusNames=SZO_16580;
OS   Streptococcus equi subsp. zooepidemicus (strain H70).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=553483;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H70;
RX   PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA   Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA   Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA   Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA   Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA   Maskell D.J., Parkhill J., Waller A.S.;
RT   "Genomic evidence for the evolution of Streptococcus equi: host
RT   restriction, increased virulence, and genetic exchange with human
RT   pathogens.";
RL   PLoS Pathog. 5:E1000346-E1000346(2009).
CC   -!- FUNCTION: Removes N-terminal dipeptides sequentially from polypeptides
CC       having unsubstituted N-termini provided that the penultimate residue is
CC       proline. {ECO:0000255|HAMAP-Rule:MF_00698}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00698};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00698}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00698}.
CC   -!- SIMILARITY: Belongs to the peptidase S15 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00698}.
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DR   EMBL; FM204884; CAX00420.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0MEP5; -.
DR   SMR; C0MEP5; -.
DR   ESTHER; strs7-pepx; Lactobacillus_peptidase.
DR   MEROPS; S15.001; -.
DR   EnsemblBacteria; CAX00420; CAX00420; SZO_16580.
DR   KEGG; seq:SZO_16580; -.
DR   PATRIC; fig|40041.11.peg.1779; -.
DR   eggNOG; COG2936; Bacteria.
DR   HOGENOM; CLU_011800_0_0_9; -.
DR   OMA; LYTASPY; -.
DR   Proteomes; UP000001368; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   HAMAP; MF_00698; Aminopeptidase_S15; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR008252; Pept_S15_Xpro.
DR   InterPro; IPR015251; PepX_N_dom.
DR   InterPro; IPR036313; PepX_N_dom_sf.
DR   InterPro; IPR000383; Xaa-Pro-like_dom.
DR   InterPro; IPR013736; Xaa-Pro_dipept_C.
DR   Pfam; PF02129; Peptidase_S15; 1.
DR   Pfam; PF08530; PepX_C; 1.
DR   Pfam; PF09168; PepX_N; 1.
DR   PRINTS; PR00923; LACTOPTASE.
DR   SMART; SM00939; PepX_C; 1.
DR   SMART; SM00940; PepX_N; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   SUPFAM; SSF81761; SSF81761; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Cytoplasm; Hydrolase; Protease; Serine protease.
FT   CHAIN           1..761
FT                   /note="Xaa-Pro dipeptidyl-peptidase"
FT                   /id="PRO_1000212635"
FT   ACT_SITE        349
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT   ACT_SITE        469
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT   ACT_SITE        499
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
SQ   SEQUENCE   761 AA;  86163 MW;  EA1A4E4E10F48E62 CRC64;
     MRYNQLSYIP TSLETAVAEL QALGFAVQQE QAPKESFAIF LRKLFFHFQD TDYPLSHMIA
     TKELDLLSFL ASDEALTKEV FDLVALQVLG FIPAVDFTDT QDFIQKIGFP IVFDSQQLLL
     NLHQLLATRQ KSGVTLIDSL VSQGLLPMDN CYHYFNGKAL ATFDTTSLIR EVVYVEAPLD
     TDQDGQLDLI KVNIIRPKAS TAIPSMMTAS PYHQGINETA NDKKLHRMEG ELSPKAPRRI
     TVEPTDFQPL ATKPSRLPVN ECQETFSHIS SYTLNDYFLA RGFANLYVSG VGTAGSTGFM
     TSGDYAQIES FKAVIDWLNG RATAYTSHKR DYQIKADWSN GLVATTGKSY LGTMSTGLAT
     TGVDGLAVII AEAAISSWYD YYRENGLVCS PGGYPGEDLD VLTELTYSRN LLPGDYLRHN
     DHYQELLSQQ SQALDRQSGD YNQFWHDRNY LPQADRIKCE VVYTHGLQDW NVKPRQVYNI
     FNALPDSLGK HLFLHHGEHV YMHNWQSIDF REAMNALLCQ KMLGQNNGFT LPTIIWQDNQ
     KEQTWKELTA FGGHSKRQIA LGEDHVLIDN HYGEEDFKRY GKDFRAFKAE LFEGKANQAV
     IDILLEEDLP INGQACLKLK LKSSENKGIL SAQLLDYGKK KRFGDLPAIL ELDSIDNGQQ
     FAREALKELP FKDSPYRVVT KGVLNLQHRS GLLTIEDIPN DQWISITFHL QPTIYHMAKG
     DTLRVVLYTT DFEHTIRDNS NYALTLDLEQ SYLLIPTDEE E