ID   PEPX_STRT1              Reviewed;         755 AA.
AC   Q5LYA9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=str1672;
OS   Streptococcus thermophilus (strain CNRZ 1066).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=299768;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNRZ 1066;
RX   PubMed=15543133; DOI=10.1038/nbt1034;
RA   Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA   Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA   Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA   Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT   "Complete sequence and comparative genome analysis of the dairy bacterium
RT   Streptococcus thermophilus.";
RL   Nat. Biotechnol. 22:1554-1558(2004).
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; CP000024; AAV63201.1; -; Genomic_DNA.
DR   RefSeq; WP_011227515.1; NC_006449.1.
DR   AlphaFoldDB; Q5LYA9; -.
DR   SMR; Q5LYA9; -.
DR   ESTHER; strtr-pepx; Lactobacillus_peptidase.
DR   MEROPS; S15.001; -.
DR   KEGG; stc:str1672; -.
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..755
FT                   /note="Xaa-Pro dipeptidyl-peptidase"
FT                   /id="PRO_1000045495"
FT   ACT_SITE        348
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT   ACT_SITE        468
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT   ACT_SITE        498
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
SQ   SEQUENCE   755 AA;  85618 MW;  1D8D603B60F47F43 CRC64;
     MKFNQFSYIP VSPETAYQEL RSLGFEVSLD ASAKANFESF VRKYFLFFED TDLALKNWIA
     DPETDLLSFF QSDRPLTAEV FGLVALQLLG FVPNVDFTDS VAFLEKMAFP IAFDGSLNNL
     HQLLATRTQS GNTLIDQLVA QDLIPISNDY VFFNGKSLAT FDTNQLHREV VYVETPVDTD
     KDGLLDLVKV TILRPNVDFP VPAMMTASPY QQGTNEPSSD KLTHKMEGDL LVKPAGKISL
     SRPEIKAPEA DLTPINPVTK AEERFAHTDT YTLNDYMLAR GVASIYVSGV GTFNSEGFMT
     SGDYQQVLAY KAVIDWLNGR ARAFTSRSRQ HTITADWASG KVTTTGLSYL GTMSNALATT
     GVDGLEMVIA EAGISSWYDY YRENGLLVSP GGYPGEDLDT LTEFTYSRAL LAGEYLRHQK
     DYEAYLNELS TDIDRKHGDY NQFWHDRNYV QFADRVKATV VFTHGSQDWN VKPINVYQMF
     RALPKSLEKH LFFHNGAHVY MNAWQSIDFR ESMNALICQK LLGLDNGYTL PTVIWQNNQS
     EQTWEVLDNF GHDNGKHIQL GKSEASIANH YEEEIFAKYG KAYQSFKDDL FMDKANAITL
     DFELDQDIQI NGRVHLELRV KSSTNRGLIS AQVLEMGDKK YLAPIPAPKR MSLDNGRLFK
     EEALRELPFK QAKYRVITKG HLNLQNRKDL LSIENVTPNE WMTIGLDLQP TIYKLNKGDK
     LRLVLYTTDF EHTIRDNSDY EVTVDLSQSK MTLPY