ID   PEPX_LIGS1              Reviewed;         801 AA.
AC   Q1WRZ1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=LSL_1534;
OS   Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=362948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCC118;
RX   PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA   Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA   Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K.,
RA   Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.;
RT   "Multireplicon genome architecture of Lactobacillus salivarius.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(2006).
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; CP000233; ABE00338.1; -; Genomic_DNA.
DR   RefSeq; WP_011476404.1; NC_007929.1.
DR   RefSeq; YP_536421.1; NC_007929.1.
DR   AlphaFoldDB; Q1WRZ1; -.
DR   SMR; Q1WRZ1; -.
DR   STRING; 362948.LSL_1534; -.
DR   ESTHER; lacs1-PEPX; Lactobacillus_peptidase.
DR   MEROPS; S15.001; -.
DR   PRIDE; Q1WRZ1; -.
DR   EnsemblBacteria; ABE00338; ABE00338; LSL_1534.
DR   KEGG; lsl:LSL_1534; -.
DR   PATRIC; fig|362948.14.peg.1625; -.
DR   HOGENOM; CLU_011800_0_0_9; -.
DR   OMA; LYTASPY; -.
DR   Proteomes; UP000006559; Chromosome.
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; Reference proteome;
KW   Serine protease.
FT   CHAIN           1..801
FT                   /note="Xaa-Pro dipeptidyl-peptidase"
FT                   /id="PRO_1000045484"
FT   ACT_SITE        371
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT   ACT_SITE        491
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT   ACT_SITE        522
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
SQ   SEQUENCE   801 AA;  91114 MW;  92E53B73A6491201 CRC64;
     MKFNQFAHVK VPFEQKLAEL NRIAFLHAGD EDLASNHIYR LFLERAFPNF KTEAAKNHAL
     SNLAATENAD ILTYLNSSKI NARVFYAVGL QLLGFEAELD FDLKDPFSAM DKLNLPYQKE
     IHHRDDVINA WYDLLCTSTK KGQNLLDILA NRGYFTQFYQ LNLTEPIFFN GKAQPVFDTN
     KLIHEVVYVE SELDTDQDGK RDLLKVIITR PAMTDNGMKV PTIFTASPYY LGTNDASAEK
     MMHSVDLPIT RKEVKPLSYQ DIEYHKPETK LPKKRPVVIS TKNAEESWEH LFTYTFNDYM
     LARGFAVVYS GGVGTLDSDG YRTCGDEAET LGAKDVVEWL NGKRTAFTTK EANKAIPAWW
     SNGKVAMTGK SYLGTLATAA ATTGVAGLET IISEAAISSW YDYYREGGLV IAPGGFPGED
     ADILAEECFS RQKSAGDYNH SKDGFNKFLS TITKDQDRTT GNYNTFWDAR NYLKDVGNIK
     CDIVMVHGLN DWNVKLKNVF NLYNKLGDVE VTKKLILHQG QHIYINNFQS LDFTDMMNLW
     LSHKLYGVEN NAKELLPDIL VQNNTKESTW ETYSSWQSKN FTKLYLNSDS LSAQKKENQT
     LEFSDHLPET TFKHYQTDIA NWKEEILAST SPKLETNRLI LTSKPLKHET LLKGVAKIKL
     KIASQLDHGL VSVKLVDYGD AKRLGATPTI LERRGLDLGY HWKEDNLVEF KLAKETPFKM
     ITQAHLNLQN RHNDFSTDEL EANKFYDVEI TTQPMFYHLP KGHKLGLVIY ATDMEMTLQG
     NEENSYRIDT TGSYCLLPIE E