ID   PEPX_STRTR              Reviewed;         755 AA.
AC   Q8GMC0;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 82.
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};
OS   Streptococcus thermophilus.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ACA-DC 4;
RX   PubMed=12067374; DOI=10.1046/j.1365-2672.2002.01659.x;
RA   Anastasiou R., Papadelli M., Georgalaki M.D., Kalantzopoulos G.,
RA   Tsakalidou E.;
RT   "Cloning and sequencing of the gene encoding X-prolyl-dipeptidyl
RT   aminopeptidase (PepX) from Streptococcus thermophilus strain ACA-DC 4.";
RL   J. Appl. Microbiol. 93:52-59(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; AY055853; AAL17713.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8GMC0; -.
DR   SMR; Q8GMC0; -.
DR   STRING; 322159.STER_1633; -.
DR   ESTHER; strtr-pepx; Lactobacillus_peptidase.
DR   MEROPS; S15.001; -.
DR   eggNOG; COG2936; Bacteria.
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_0000220235"
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;  85632 MW;  9BF73658F4C444AF 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 TAIDRKHGDY NQFWHDRNYV QFADRVKATV VFTHGSQDWN VKPINVYQMF
     RALPKSLEKH LFFHNGAHVY MNAWQSIDFR ESMNALICQK LLGLDNGYTL PTVIWQNNQS
     EQTWEVLDNF GHDNGKHIQL GKSEASIANH YEEEIFAKYG KAYQSFKDDL FMDKANAITL
     DFELDQDIQI NGRVHLELRV KSSTNRGLIS AQVLEMGDKK YLAPIPELKR MSLDNGRLFK
     EEALRELPFK QAKYRVITKG HLNLQNRKDL LSIENVTPNE WMTIGLDLQP TIYKPNKGDK
     LRLVLYTTDF EHTIRDNSDY EVTVDLSQSK MTLPY