ID   PEPX_STRA3              Reviewed;         761 AA.
AC   Q8E3H8;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=gbs1781;
OS   Streptococcus agalactiae serotype III (strain NEM316).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=211110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEM316;
RX   PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA   Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA   Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT   "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT   neonatal disease.";
RL   Mol. Microbiol. 45:1499-1513(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}.
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DR   EMBL; AL766853; CAD47440.1; -; Genomic_DNA.
DR   RefSeq; WP_001270177.1; NC_004368.1.
DR   AlphaFoldDB; Q8E3H8; -.
DR   SMR; Q8E3H8; -.
DR   STRING; 211110.gbs1781; -.
DR   ESTHER; strag-pepx; Lactobacillus_peptidase.
DR   EnsemblBacteria; CAD47440; CAD47440; CAD47440.
DR   KEGG; san:gbs1781; -.
DR   eggNOG; COG2936; Bacteria.
DR   HOGENOM; CLU_011800_0_0_9; -.
DR   OMA; LYTASPY; -.
DR   Proteomes; UP000000823; 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_0000220224"
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;  86844 MW;  CFB3D0F7B1CEE1E0 CRC64;
     MRYNQFSYIP TKPNEAFEEL KGLGFPLNKK NSDKANLEAF LRHSFLNQTD TDYALSLLIV
     DAKTDALTFF KSNSDLTLEN LQWIYLQLLG FVPFVDFKDP KAFLQDINFP VSYDNIFQSL
     HHLLACRGKS GNTLIDQLVA DGLLHADNHY HFFNGKSLAT FNTNQLIREV VYVEISLDTM
     SSGEHDLVKV NIIRPTTEHT IPTMMTASPY HQGINDPAAD QKTYQMEGAL AVKQPKHIQV
     DTKPFKEEVK HPSKLPISPA TESFTHIDSY SLNDYFLSRG FANIYVSGVG TAGSTGFMTS
     GDYQQIQSFK AVIDWLNGKV TAFTSHKRDK QVKADWSNGL 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