ID   PEPX_STRA5              Reviewed;         761 AA.
AC   Q8DXW0;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=SAG1736;
OS   Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=208435;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-611 / 2603 V/R;
RX   PubMed=12200547; DOI=10.1073/pnas.182380799;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA   Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA   Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D.,
RA   Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A.,
RA   Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T.,
RA   Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D.,
RA   Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT   "Complete genome sequence and comparative genomic analysis of an emerging
RT   human pathogen, serotype V Streptococcus agalactiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE009948; AAN00599.1; -; Genomic_DNA.
DR   RefSeq; NP_688726.1; NC_004116.1.
DR   RefSeq; WP_001270172.1; NC_004116.1.
DR   AlphaFoldDB; Q8DXW0; -.
DR   SMR; Q8DXW0; -.
DR   STRING; 208435.SAG1736; -.
DR   ESTHER; strag-pepx; Lactobacillus_peptidase.
DR   EnsemblBacteria; AAN00599; AAN00599; SAG1736.
DR   KEGG; sag:SAG1736; -.
DR   PATRIC; fig|208435.3.peg.1744; -.
DR   HOGENOM; CLU_011800_0_0_9; -.
DR   OMA; LYTASPY; -.
DR   Proteomes; UP000000821; 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..761
FT                   /note="Xaa-Pro dipeptidyl-peptidase"
FT                   /id="PRO_0000220225"
FT   ACT_SITE        347
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT   ACT_SITE        467
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT   ACT_SITE        497
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
SQ   SEQUENCE   761 AA;  86845 MW;  8A6F266D63D02CB2 CRC64;
     MRYNQFSYIP TKPNEAFEEL KGLGFPLNKK NSDKANLEAF LRHSFLNQTD TDYALSLLIV
     DAKTDALTFF KSNSDLTLEN LQWIYLQLLG FIPFVDFKDP KAFLQDINFP VSYDNIFQSL
     HHLLACRGKS GNTLIDQLVA DGLLHADNHY HFFNGKSLAT FNTNQLIREV VYVETSLDTM
     SSGEHDLVKV NIIRPTTEHT IPTMMTASPY HQGINDPAAD QKTYQMEGAL AVKQPKHIQV
     DTKPFKEEVK HPSKLPISPA TESFTHIDSY SLNDYFLSRG FANIYVSGVG TAGSTGFMTS
     GDYQQIQSFK AVIDWLNGKV TAFTSHKRDK QVKANWSNGL VATTGKSYLG TMSTGLATTG
     VEGLKVIIAE AAISTWYDYY RENGLVCSPG GYPGEDLDVL TELTYSRNLL AGDYIKNNDC
     YQALLNEQSK AIDRQSGDYN QYWHDRNYLT HVNNVKSRVV YTHGLQDWNV KPRHVYKVFN
     ALPQTIKKHL FLHQGQHVYM HNWQSIDFRE SMNALLSQEL LGIDNHFQLE EVIWQDNTTE
     QTWQVLDAFG GNHQEQIGLG DSKKLIDNHY DKEAFDTYCK DFNVFKNDLF KGNNKTNQIT
     INLPLKKNYL LNGQCKLHLR VKTSDKKAIL SAQILDYGPK KRFKDTPTIK FLNSLDNGKN
     FAREALRELP FTKDHYRVIS KGVLNLQNRT DLLTIEAIEP EQWFDIEFSL QPSIYQLSKG
     DNLRIILYTT DFEHTIRDNA SYSITVDLSQ SYLTIPTNQG N