ID   PEPX_LEVBA              Reviewed;         811 AA.
AC   Q03PM5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=LVIS_1782;
OS   Levilactobacillus brevis (strain ATCC 367 / BCRC 12310 / CIP 105137 / JCM
OS   1170 / LMG 11437 / NCIMB 947 / NCTC 947) (Lactobacillus brevis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Levilactobacillus.
OX   NCBI_TaxID=387344;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 367 / BCRC 12310 / CIP 105137 / JCM 1170 / LMG 11437 / NCIMB
RC   947 / NCTC 947;
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; CP000416; ABJ64847.1; -; Genomic_DNA.
DR   RefSeq; WP_011668398.1; NC_008497.1.
DR   AlphaFoldDB; Q03PM5; -.
DR   SMR; Q03PM5; -.
DR   STRING; 387344.LVIS_1782; -.
DR   ESTHER; lacba-pepx; Lactobacillus_peptidase.
DR   EnsemblBacteria; ABJ64847; ABJ64847; LVIS_1782.
DR   KEGG; lbr:LVIS_1782; -.
DR   PATRIC; fig|387344.15.peg.1692; -.
DR   eggNOG; COG2936; Bacteria.
DR   HOGENOM; CLU_011800_0_0_9; -.
DR   OMA; LYTASPY; -.
DR   OrthoDB; 327988at2; -.
DR   Proteomes; UP000001652; 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..811
FT                   /note="Xaa-Pro dipeptidyl-peptidase"
FT                   /id="PRO_1000045478"
FT   ACT_SITE        377
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT   ACT_SITE        497
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT   ACT_SITE        528
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
SQ   SEQUENCE   811 AA;  90917 MW;  E1CFED7790B0BADF CRC64;
     MRNQQFAIRP TTLDQARVEL QQIHFLDDTN LSFTTPSDLL RDFYDRSWPE YTTSSVVAQQ
     LSNLMATPET DGLTYLTTHE QVPVDVFYNL ALQRLGFAVD LDFQLTDPLA AMTKIQLPVA
     DHEGTTFTLN ELMNAWYVLL TTHNKTGQTF LDQLTTHGYF APLIHDNSVP KPLIFNGKAQ
     AVFDTTQLIH EVVYVESPQD TDHDGHRDLL KAEIIRPAET ANGLKVPVLY TASPYNQGTN
     DEAGEALTHN VNVPLTAKQP AATTLADVTA ESVTTPLPDA RPVTATTHTA AETFAREQSY
     TLNDYFLARG FAVVYAAGIG TKDSDGLRTT GDPEETTSTI AIIEWLAGNR TAFTTRNATQ
     AIPAWWSNHQ VAMTGRSYLG TLATAAATTG VAGLKTVISE AAISNWYDYY RDGGLVVAPG
     GFPGEDADVL AEETFSRQLL AGDYHRIQEK WQHQLAAITQ NQDRVTGNYN RFWDARNYLK
     NAKNIKADLL LVHGLNDWNV KPRNVNNLWR AVRDLPVTKK LILHQGQHIY INAFRSIDYT
     DIVNLWLTHE LLGVDNHAET LLPNVIIQDN VTPETWQAYP DWDAPSNPVQ HFNLQADELV
     APSDHIPAAA TSFNDQLPVD QFNHYTHHID EWQADLLGDK HNAMFKHRLL FKSAVLTDDL
     VLDGRPTIDL QVAVNQPLGL LSFQLVDYGD AKRLGVSPTP LRIRLDEGYR WREDNLREFT
     VAATTPWKMI TKGHRNLQNR TNAYQVDELK PNTFYDLSVT LQPTHYRLLA GHQLGLVIYA
     TDFGMTVRGN QDLQYSIQLG QSALHVPFIT D