ID   PEPX_STRU0              Reviewed;         758 AA.
AC   B9DVM1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=SUB1574;
OS   Streptococcus uberis (strain ATCC BAA-854 / 0140J).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=218495;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-854 / 0140J;
RX   PubMed=19175920; DOI=10.1186/1471-2164-10-54;
RA   Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A.,
RA   Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R.,
RA   Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D.,
RA   Parkhill J.;
RT   "Evidence for niche adaptation in the genome of the bovine pathogen
RT   Streptococcus uberis.";
RL   BMC Genomics 10:54-54(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; AM946015; CAR43372.1; -; Genomic_DNA.
DR   RefSeq; WP_015911880.1; NC_012004.1.
DR   AlphaFoldDB; B9DVM1; -.
DR   SMR; B9DVM1; -.
DR   STRING; 218495.SUB1574; -.
DR   ESTHER; stru0-pepx; Lactobacillus_peptidase.
DR   PRIDE; B9DVM1; -.
DR   EnsemblBacteria; CAR43372; CAR43372; SUB1574.
DR   KEGG; sub:SUB1574; -.
DR   eggNOG; COG2936; Bacteria.
DR   HOGENOM; CLU_011800_0_0_9; -.
DR   OMA; LYTASPY; -.
DR   OrthoDB; 327988at2; -.
DR   Proteomes; UP000000449; 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; Reference proteome;
KW   Serine protease.
FT   CHAIN           1..758
FT                   /note="Xaa-Pro dipeptidyl-peptidase"
FT                   /id="PRO_1000192762"
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   758 AA;  86360 MW;  6E338C0EB0332424 CRC64;
     MRYNQFSYIK TDGQVAKKEL ENLGFHFPIS NKPKEIFRSF LNTYFFQSSD KDYQIASFIA
     DFETDLLSFF NADKPLTKEI FDMVSLQLLG FIPGFDFENL KEFTSQIAFP VPFNENDLFA
     SIHHLLGTRH KNGMLLIDDL ISKGFLGPDN TYHFFNGKTL ATFDTSQLIK EVVYVEAPID
     SDNDGKSDLI KVMILRPRSQ KQIPTVMTAS PYHQGINEVA NDKKLHSMQT DLPLKEAHKI
     HVADASISTL VCENADLPIT ENTEQFSYID SYTLNDYFLS RGFANIYVSG VGTADSDGFM
     TSGDYVQIES FKAIIDWLNG RAKAFTSHKR EAYVLANWSN GKVATTGKSY LGTMSNGLAT
     TGVEGLEVII AEAAISSWYD YYRENGLICS PGGYPGEDLD VLTELTYSRS LHAGDFLRQK
     EKYYQLLNQQ SQAIDRDSGD YNQFWHDRNY LPNAKNVTCE VVFTHGLQDW NVKPRQVYNM
     FNALPGSVAK HLFLHHGQHV YMHNWQSIDF KECMNALLCQ KLLGIASNFQ LPAILWQNNQ
     EEQKWQSLEE FGTSNTFRIP LGEGFAKISN QYSTETFERY SKDFKSFKRD LFSGKANQLS
     LEFPLDQDLQ LNGEAILHLS LTSSVSKGLI SAQLLDKGLK KRLGDTPTIL DLKVMDNGQN
     FSREDLKELP MRESTERVIS KGVLNLQNRD GLLEVQSVEA DQWLSFDFKL QPSLYQLRKG
     DCLQVLLYTT DFEHTVRDNS DYELRINLEK SYLSLPIA