ID   PEPX_STRPG              Reviewed;         760 AA.
AC   A2RCP2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=SpyM50273;
OS   Streptococcus pyogenes serotype M5 (strain Manfredo).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=160491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Manfredo;
RX   PubMed=17012393; DOI=10.1128/jb.01227-06;
RA   Holden M.T.G., Scott A., Cherevach I., Chillingworth T., Churcher C.,
RA   Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Moule S., Mungall K., Quail M.A., Price C., Rabbinowitsch E., Sharp S.,
RA   Skelton J., Whitehead S., Barrell B.G., Kehoe M., Parkhill J.;
RT   "Complete genome of acute rheumatic fever-associated serotype M5
RT   Streptococcus pyogenes strain Manfredo.";
RL   J. Bacteriol. 189:1473-1477(2007).
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; AM295007; CAM29615.1; -; Genomic_DNA.
DR   RefSeq; WP_011888609.1; NC_009332.1.
DR   AlphaFoldDB; A2RCP2; -.
DR   SMR; A2RCP2; -.
DR   ESTHER; strpy-PEPXP; Lactobacillus_peptidase.
DR   KEGG; spf:SpyM50273; -.
DR   HOGENOM; CLU_011800_0_0_9; -.
DR   OMA; LYTASPY; -.
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..760
FT                   /note="Xaa-Pro dipeptidyl-peptidase"
FT                   /id="PRO_1000045492"
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   760 AA;  86816 MW;  D572407C18FFC744 CRC64;
     MRYNQFSYIP TSLERAAEEL KELGFDLDLQ KTAKVNLESF LRKLFFHYPD SDYPLSHLIT
     KNDMDALSFF QSEQELSKEV FDLLALQVLG FIPGVDFTEA DAFLDKLAFP IHFDETEIIK
     HIHHILATRC KSGMTLIDDL VSQGMLTMDN DYHFFNGKSL ATFDTSQLIR EVVYVEAPLD
     TDQDGQLDLI KVNIIRPQSQ KPLPTLMTPS PYHQGINEVA NDKKLYRMEK ELVVKKRRQI
     TVEDRDFIPL ETQPCKLPIG QNLEIFSYIN SYSLNDYFLA RGFANIYVSG VGTAGSTGFM
     TSGDYAQIES FKAVIDWLNG RATAYTSHSK THQVRADWAN GLVCTTGKSY LGTMSTGLAT
     TGVDGLAMII AESAISSWYN YYRENGLVCS PGGYPGEDLD VLTELTYSRN LLAGDYLRHN
     DRYQELLNQQ SQALDRQSGD YNQFWHDRNY LKNAHQIKCD VVYTHGLQDW NVKPRQVYEI
     VNALPSTINK HLFLHQGEHV YMHNWQSIDF RESMNVLLCQ KLLGLANDFS LPEMIWQDNT
     CPQNWQERKV FGTSTIKELD LGQELLLIDN HYGEDEFKAY GKDFRAFKAA LFKGKANQAL
     VDILLEEDLP INGEIVLQLK VKSSENKGLL SAQILDYGKK KRLGDLPIAL TQSSIDNGQN
     FSREPLKELP FREDSYRVIS KGFMNLQNRN NLSSIETIPN NKWMTVRLPL QPTIYHLEKG
     DTLRVILYTT DFEHTVRDNS NYALTIDLSQ SQLIVPIASN