ID   PEPX_STREM              Reviewed;         761 AA.
AC   B4U108;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=Sez_0319;
OS   Streptococcus equi subsp. zooepidemicus (strain MGCS10565).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=552526;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGCS10565;
RX   PubMed=18716664; DOI=10.1371/journal.pone.0003026;
RA   Beres S.B., Sesso R., Pinto S.W.L., Hoe N.P., Porcella S.F., Deleo F.R.,
RA   Musser J.M.;
RT   "Genome sequence of a lancefield group C Streptococcus zooepidemicus strain
RT   causing epidemic nephritis: new information about an old disease.";
RL   PLoS ONE 3:E3026-E3026(2008).
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; CP001129; ACG61695.1; -; Genomic_DNA.
DR   RefSeq; WP_012514974.1; NC_011134.1.
DR   AlphaFoldDB; B4U108; -.
DR   SMR; B4U108; -.
DR   ESTHER; stre4-pepx; Lactobacillus_peptidase.
DR   MEROPS; S15.001; -.
DR   PRIDE; B4U108; -.
DR   EnsemblBacteria; ACG61695; ACG61695; Sez_0319.
DR   KEGG; sez:Sez_0319; -.
DR   HOGENOM; CLU_011800_0_0_9; -.
DR   OMA; LYTASPY; -.
DR   Proteomes; UP000001873; 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_1000132341"
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;  86259 MW;  90380E993D1B730D 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
     DHYQQLLSQQ SQALERQSGN YNQFWHDRNY LPQADHIKCE VVYTHGLQDW NVKPRQVYNI
     FNALPDGLGK HLFLHHGEHV YMHNWQSIDF REAMNALLCQ KMLGQNNGFT LPTIIWQDNQ
     KEQTWKELTA FGGHSKRQIA LGEDHVLIDN HYGEEDFKRY SKDFRAFKAE LFEGKANQAV
     IDILLEEDLP INGQACLKLK LKSSENKGIL SAQLLDYGKK KRFADIPAIL ELDSIDNGQQ
     FAREALKELP FKDSPYRVVT KGVLNLQHRS NLLTIEDIPN DQWMTITFHL QPTIYHMAKG
     DTLRVVLYTT DFEHTIRDNS NYALTLDLEQ SYLLIPTDEE E