ID   PEPX_PEDPA              Reviewed;         812 AA.
AC   Q03H46;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=PEPE_0380;
OS   Pediococcus pentosaceus (strain ATCC 25745 / CCUG 21536 / LMG 10740 /
OS   183-1w).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Pediococcus.
OX   NCBI_TaxID=278197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25745 / CCUG 21536 / LMG 10740 / 183-1w;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(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; CP000422; ABJ67476.1; -; Genomic_DNA.
DR   RefSeq; WP_002832821.1; NC_008525.1.
DR   AlphaFoldDB; Q03H46; -.
DR   SMR; Q03H46; -.
DR   STRING; 278197.PEPE_0380; -.
DR   ESTHER; pedpa-pepx; Lactobacillus_peptidase.
DR   PRIDE; Q03H46; -.
DR   EnsemblBacteria; ABJ67476; ABJ67476; PEPE_0380.
DR   GeneID; 33062624; -.
DR   KEGG; ppe:PEPE_0380; -.
DR   eggNOG; COG2936; Bacteria.
DR   HOGENOM; CLU_011800_0_0_9; -.
DR   OMA; LYTASPY; -.
DR   OrthoDB; 327988at2; -.
DR   Proteomes; UP000000773; 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..812
FT                   /note="Xaa-Pro dipeptidyl-peptidase"
FT                   /id="PRO_1000045485"
FT   ACT_SITE        372
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT   ACT_SITE        492
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT   ACT_SITE        523
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
SQ   SEQUENCE   812 AA;  92354 MW;  35AE61D64CC21438 CRC64;
     MKNNQFGRIR LDRTTELEEL KNIHFIDADL LADPKAQLKD FLKRSCLVSN SEATFQQKLS
     NLLATPDQTM AAFFESDQPL TLEIFILLEL QLLQFEADTD YQIEDPLSAI SKIQLPELDL
     KNFETSADVA HAWYNLLTTH TKNGEVYLDR LTQQGYFVSF YPTTTKPLFF NGKAQAVFDP
     HQLIREVVYV EAPLDTDHDG QRDLLKAEIL RPAQTAHGYQ APVLYTASPY NQGTNDSYGE
     AITHNVDVPL TEKAVQKISK SDVTAEPFSQ TLPAERKVAG MATKASETFA REQPYTLNNY
     FLSRGFAVVY AAGIGTRDSD GLRDTGSVEE TISTTAIIEW LAGNRRAFTN KTDNLEIKAS
     WSNHKIAMTG RSYLGTLATA AATTGVEGLE TIISEAAISS WYDYYRDGGL VAAPDTFQGE
     DMDVLAAEVL SRKHDAGDYL GIKAHFDQIL KRIEKDQDRD SGNYSKYWDS KNYLNNVKNI
     KADIIMVHGL NDWNVKPRNV GKLWNAVRDL PINKKIILHQ GQHIYINAFR SIDFTDMMNL
     WLSYKLFDVQ NGANEVLPNV IIQDNVEPET WNTYQDWQAA DDEIREFTLQ AKTLVDRASE
     TKNEAASFRD SLDPEFFEMY KNDLKHWHTD LLNTEHATNG KNQMRNNRLI FKTAQTKEDW
     LIDGTPEVSV NVAVNQPFGM LSFQLVDFGD AKRLNPSPSI LQPRSLSGSF DWRTDDLREF
     TLQNAVTPWK MISKGHINLQ NRTNNYCVDE VKPHQFYDVK LELQPTFYRL LAGHQLGLVI
     YATDFETTIR GNQELLYSLQ LNQSHLKIKL AH