ID   PEPX_LACLS              Reviewed;         763 AA.
AC   Q02W78;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=LACR_2342;
OS   Lactococcus lactis subsp. cremoris (strain SK11).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=272622;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK11;
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; CP000425; ABJ73794.1; -; Genomic_DNA.
DR   RefSeq; WP_011677123.1; NC_008527.1.
DR   AlphaFoldDB; Q02W78; -.
DR   SMR; Q02W78; -.
DR   ESTHER; lacla-pepx; Lactobacillus_peptidase.
DR   MEROPS; S15.001; -.
DR   PRIDE; Q02W78; -.
DR   EnsemblBacteria; ABJ73794; ABJ73794; LACR_2342.
DR   KEGG; llc:LACR_2342; -.
DR   HOGENOM; CLU_011800_0_0_9; -.
DR   OMA; LYTASPY; -.
DR   Proteomes; UP000000240; 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; Serine protease.
FT   CHAIN           1..763
FT                   /note="Xaa-Pro dipeptidyl-peptidase"
FT                   /id="PRO_1000045483"
FT   ACT_SITE        348
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT   ACT_SITE        468
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT   ACT_SITE        498
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
SQ   SEQUENCE   763 AA;  87746 MW;  D1A9C471E1F2FCB9 CRC64;
     MRFNHFSIVD KNFDEQLAEL DQLGFRWSVF WDEKKILKDF LIQSPSDMTD LQATAELDVI
     EFLKSSIELD WEIFWNIALQ LLDFVPNFDF EIGKAFEYAK NSNLPQIEAE MTTENIISAF
     YYLLCTRRKN GMILVEHWVS EGLLPLDNHY HFFNDKSLAT FDSSLLEREV LWVESPVDSE
     QRGENDLIKI QIIRPKSTEK LPVVMTASPY HLGINDKAND LALHDMNVEL EEKASHEIHV
     EQKLPQKLSA KAKELPIVDK APYRFTHGWT YSLNDYFLTR GFASIYVAGV GTRSSDGFQT
     SGDYQQIYSM TAVIDWLNGR ARAYTSRKKT HEIKASWANG KVAMTGKSYL GTMAYGAATT
     GVEGLEVILA EAGISSWYNY YRENGLVRSP GGFPGEDLDV LAALTYSRNL DGADFLKGNA
     EYEKRLAEMT AALDRKSGDY NQFWHDRNYL INTDKVKADV LIVHGLQDWN VTPEQAYNFW
     KALPEGHAKH AFLHRGAHIY MNSWQSIDFS ETINAYFVAK LLDRDLNLNL PPVILQENSK
     DQVWTMMNDF GANTQIKLPL GKTAVSFAQF DNHYDDETFK KYSKDFNVFK KDLFENKANE
     AVIDLELPSM LTINGPVELE LRLKLNDTKG FLSAQILDFG QKKRLEDKAR VKDFKVLDRG
     RNFMLDDLVE LPLVESPYQL ITKGFTNLQN QNLLTVSDLK ADEWFTIKFE LQPTIYHLEK
     ADKLRVILYS TDFEHTVRDN RKVTYEIDLS QSKLIIPIES VKN