ID   PEPX_LACDE              Reviewed;         786 AA.
AC   Q9Z5K9;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 90.
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;
DE   Flags: Fragment;
GN   Name=pepX;
OS   Lactobacillus delbrueckii subsp. bulgaricus.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1585;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CNRZ 397;
RA   Morel F.;
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Removes N-terminal dipeptides sequentially from polypeptides
CC       having unsubstituted N-termini provided that the penultimate residue is
CC       proline. {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S15 family. {ECO:0000305}.
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DR   EMBL; AJ012302; CAB38074.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9Z5K9; -.
DR   SMR; Q9Z5K9; -.
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-EC.
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..786
FT                   /note="Xaa-Pro dipeptidyl-peptidase"
FT                   /id="PRO_0000220217"
FT   ACT_SITE        357
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        476
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        507
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   786 AA;  87627 MW;  90578E5DA8F6447A CRC64;
     AYVETSPEKA TEELLAINFL PENYSSLSFS ELLAVLTGNV LAEATTRQAK DAKLAEFAVD
     DQTDLAAFLL DTPTAITASQ FANVALQLLG YHPNYDYSLT DPLTCGEKHA LPAFKDLTSK
     EELIFAFYRL LNTRSKNGQI LLDVMAGKGY FTQFWGEGKF MLFNGKSLPV FDTSQVIREV
     VYVQSDLDTD GDGKGDLLPV TVFRPVESQD QLKVPALYTA SPYFGGIIDN VKTNHNVDEN
     LTDATTWTNP KYVAKPLVKS PAPSGQDVPA TELATGQSSY GLNEYLLARG FASVFSGAIG
     NRHGDGIRIT GSPEETISQK EVIEWLTGDR VAYTDRTRRF ETKASWCSGN VGMTGRSYLG
     TLQIAIATTG VKGLKTVVSE AAISSWYDYY REHGLVIAPS ECQGEDMDKL AEVCQSNLWD
     GGNFTAKKAY EAEQAELLAA QDRATGQYSD FWESRNYRHH ADGIKCSWIS VHGLNDWNVK
     PKNVYKIWQK VKQLPVESHL FLHQGPHYNM NNLVSIDFTD LMNLWFVHEL LEVENGAYEQ
     WPKVMIQDNL EADKWHAESD WANDLGQASL YSPTADGYLS TVENGTGQLT FTDLGGTEFK
     KAGISETDWE YQFISGEKKW AKASLRFESE EFLHPTTLVG RPKVQVRVAA NKTVGQLSVA
     LVDLGTRQRL TATPKIFARG NQPFAYRFEA DSLQEFVPDK ATKAKLITKA HMNLQNYQDM
     KQPSKLEAGQ FVDLEFELQP TYYTLPAGAK LCLIIYSTDQ GMTKRPLETE DYTVDLAGTA
     LLLYRK