ID   PEPX_STRGN              Reviewed;         759 AA.
AC   Q93M42;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Xaa-Pro dipeptidyl-peptidase;
DE            EC=3.4.14.11;
DE   AltName: Full=Sg-xPDPP;
DE   AltName: Full=X-Pro dipeptidyl-peptidase;
DE   AltName: Full=X-prolyl-dipeptidyl aminopeptidase;
DE            Short=X-PDAP;
GN   Name=pepX;
OS   Streptococcus gordonii.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1302;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=FSS2;
RX   PubMed=11500422; DOI=10.1128/iai.69.9.5494-5501.2001;
RA   Goldstein J.M., Banbula A., Kordula T., Mayo J.A., Travis J.;
RT   "Novel extracellular x-prolyl dipeptidyl-peptidase (DPP) from Streptococcus
RT   gordonii FSS2: an emerging subfamily of viridans Streptococcal x-prolyl
RT   DPPs.";
RL   Infect. Immun. 69:5494-5501(2001).
CC   -!- FUNCTION: Removes N-terminal dipeptides sequentially from polypeptides
CC       having unsubstituted N-termini provided that the penultimate residue is
CC       proline.
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   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase S15 family. {ECO:0000305}.
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DR   EMBL; AY032733; AAK39633.1; -; Genomic_DNA.
DR   RefSeq; WP_048776360.1; NZ_LR594041.1.
DR   AlphaFoldDB; Q93M42; -.
DR   SMR; Q93M42; -.
DR   ESTHER; strgo-Q93M42; Lactobacillus_peptidase.
DR   SABIO-RK; Q93M42; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR   GO; GO:0005576; C:extracellular region; 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   1: Evidence at protein level;
KW   Aminopeptidase; Hydrolase; Protease; Secreted; Serine protease.
FT   CHAIN           1..759
FT                   /note="Xaa-Pro dipeptidyl-peptidase"
FT                   /id="PRO_0000220226"
FT   ACT_SITE        347
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        467
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        497
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   759 AA;  87115 MW;  74C9CF96483FAB44 CRC64;
     MRYNQYSYTK ASEEVMLDEL ARLGFTIQTT NSPKENLHHF LQKILFRYQD VNYVLSSWVA
     DQKTDLLTFF QSDKQLTEEV FYTVALQVLG FAPFVDFDDV TAFCKEIHFP ITYGNILENL
     YQLLNTRTKL GNTLIDQLVS EGFIPESNDY HFFNGKSLAT FSSHEAIREV VYVESRVDTD
     GDGKPDLVKV SIIRPSYEGQ VPAVMTASPY HQGTNDKASD KALHNMNVDL SCKNPRTITV
     QESSIQTIEP QGQASLVEKA EEKLGHIGSY TLNDYLLPRG FANLYVSGVG TKDSEGMMTS
     GDYQQIEAYK NVIDWLNGRC RAFTDHTRQR EIKATWSNGK VATTGISYLG TMSNGLATTG
     VDGLEVIIAE AGISSWYNYY RENGLVTSPG GYPGEDFESL TELTYSRNLL AGEYLRHNQA
     YQAYLDQQRK DLERETGDYN QFWHDRNYLI HADKVKAEVV FTHGSQDWNV KPLHVYNMFH
     ALPAHIKKHL FFHNGAHVYI NNWQSIDFRE SMNALLSKKL LGHSSDFDLP PVIWQDNSQA
     QNWMSLDDFG NQEDYSHFHL GKGSQEIRNR YSDEDYNRFA KSYQVFKNEL FEGKTQQITL
     DWTLEQDLFI NGPAKLKLRL KSSTNKGLIS AQLLDYGPAK RLTPIPSLLE PRVMDNGRYY
     MLDNLMELPF ADTPHRVITK GFLNLQNRTD LLTVEEVVPN QWMELSFELQ PTIYKLKKGD
     QLRLVLYTTD FEHTVRDKTD YHLSVDMEHS SLSLPHKKS