ID   PEPX_LACDL              Reviewed;         792 AA.
AC   P40334;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Xaa-Pro dipeptidyl-peptidase;
DE            EC=3.4.14.11;
DE   AltName: Full=X-Pro dipeptidyl-peptidase;
DE   AltName: Full=X-prolyl-dipeptidyl aminopeptidase;
DE            Short=X-PDAP;
GN   Name=pepX;
OS   Lactobacillus delbrueckii subsp. lactis.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=29397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10.
RC   STRAIN=DSM 7290 / WS87;
RX   PubMed=7765315; DOI=10.1007/bf00170433;
RA   Meyer-Barton E.C., Klein J.R., Imam M., Plapp R.;
RT   "Cloning and sequence analysis of the X-prolyl-dipeptidyl-aminopeptidase
RT   gene (pepX) from Lactobacillus delbruckii ssp. lactis DSM7290.";
RL   Appl. Microbiol. Biotechnol. 40:82-89(1993).
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.0.;
CC       Temperature dependence:
CC         Optimum temperature is 46-50 degrees Celsius.;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S15 family. {ECO:0000305}.
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DR   EMBL; Z14230; CAA78597.1; -; Genomic_DNA.
DR   PIR; S32244; S32244.
DR   RefSeq; WP_070488955.1; NZ_JACSVI010000082.1.
DR   AlphaFoldDB; P40334; -.
DR   SMR; P40334; -.
DR   ESTHER; lacdl-pepx; Lactobacillus_peptidase.
DR   MEROPS; S15.001; -.
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   1: Evidence at protein level;
KW   Aminopeptidase; Cytoplasm; Direct protein sequencing; Hydrolase; Protease;
KW   Serine protease.
FT   CHAIN           1..792
FT                   /note="Xaa-Pro dipeptidyl-peptidase"
FT                   /id="PRO_0000220218"
FT   ACT_SITE        363
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        482
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        513
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   792 AA;  88439 MW;  80DA43B8295BD181 CRC64;
     MKYNQYAYVE TSPEKATEEL LAINFLPENY SSLSFSELLA VLTGNVLAEA TTRQAKDAKL
     AEFAVDDQTD LAAFLLDTPT AITASQFANV ALQLLGYHPN YDYSLTDPLT CGKKHALPAF
     KDLTSKEELI FTFYRLLNTR SKNGQILLDV MAGKGYFTQF WGEGKFMFFN GKSLPVFDTS
     QVIREVVYVQ SDLDTDGDGK GDLLPVTVFR PVESQDQLKV PALYTASPYF GGIIDNVKTN
     HNVDENLTDA TTWTNPKYVA KPLVKSPAPS DQDVPATELA TGQSSYGLNE YLLARGFASV
     FSGAIGNRHG DGIRITGSPE ETISQKEVIE WLTGDRVAYT DRTRRFETKA SWCSGNVGMT
     GRSYLGTLQI AIATTGVKGL KTVVSEAAIS SWYDYYREHG LVVAPSECQG EDMDKLAEVC
     QSNLWDGGNF TAKKAYEAEQ AELLAAQDRA TGQYSDFWES RNYRHHTDGI KCSWISVHGL
     NDWNVKPKNV YKIWQKVKQL PVKSHLFLHQ GPHYNMNNLV SIDFTDLMNL WFVHELLEVE
     NGAYEQWPKV MIQDNLEADE WHAESDWASD LGQASLYLPT ADGDLSTVEN GTGQLTFTDL
     GGTEFKKAGI SETDWEYQFI SGEEKWAKAS LRFESEEFLH PTTLVGRPKV RVRVAANKTV
     GQLSVALVDL GTRQRLTATP KIFARGNQPF GYRFGADSLQ EFVPDKATKA KLITKAHMNL
     QNYQDMKQPS KLEAGQFVDL EFELQPTYYT LPAGAKLGLI IYSTDQGMTK RPLETEDYTV
     DLAGTALLLY RK