ID   PEPX_LACLM              Reviewed;         763 AA.
AC   A2RNK1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=llmg_2328;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
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; AM406671; CAL98891.1; -; Genomic_DNA.
DR   RefSeq; WP_011835997.1; NZ_WJVF01000005.1.
DR   AlphaFoldDB; A2RNK1; -.
DR   SMR; A2RNK1; -.
DR   STRING; 416870.llmg_2328; -.
DR   ESTHER; lacla-pepx; Lactobacillus_peptidase.
DR   MEROPS; S15.001; -.
DR   EnsemblBacteria; CAL98891; CAL98891; llmg_2328.
DR   KEGG; llm:llmg_2328; -.
DR   eggNOG; COG2936; Bacteria.
DR   HOGENOM; CLU_011800_0_0_9; -.
DR   OMA; LYTASPY; -.
DR   PhylomeDB; A2RNK1; -.
DR   BioCyc; LLAC416870:LLMG_RS11670-MON; -.
DR   Proteomes; UP000000364; 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_1000045482"
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;  87697 MW;  F89D81F88BDD7BEE CRC64;
     MRFNHFSIVD KNFDEQLAEL DQLGFRWSVF WDEKKILKDF LIQSPSDMTA LQATAELDVI
     EFLKSSIELD WEIFWNIALQ LLDFVPNFDF EIGKAFEYAK NSNLPQIEAE MTTENIISAF
     YYLLCTRRKT GMILVEHWVS EGLLPLDNHY HFFNDKSLAT FDSSLLEREV LWVESPVDSE
     QRGENDLIKI QIIRPKSTEK LPVVMTASPY HLGINDKAND LALHDMNVEL EEKTSHEIHV
     EQKLPQKLSA KAKELPIVDK APYRFTHGWT YSLNDYFLTR GFASIYVAGV GTRSSDGFQT
     SGDYQQIYSM TAVIDWLNGR ARAYTSRKKT HEIKASWANG KVAMTGKSYL GTMAYGAATT
     GVEGLELILA EAGISSWYNY YRENGLVRSP GGFPGEDLDV LAALTYSRNL DGADFLKGNA
     EYEKRLAEMT AALDRKSGDY NQFWHDRNYL INTDKVKADV LIVHGLQDWN VTPEQAYNFW
     KALPEGHAKH AFLHRGAHIY MNSWQSIDFS ETINAYFVAK LLDRDLNLNL PPVILQENSK
     DQVWTMMNDF GANTQIKLPL GKTAVSFAQF DNNYDDETFK KYSKDFNVFK KDLFENKANE
     AVIDLELPSM LTINGPVELE LRLKLNDTKG FLSAQILDFG QKKRLEDKVR VKDFKVLDRG
     RNFMLDDLVE LPLVESPYQL VTKGFTNLQN QSLLTVSDLK ADEWFTIKFE LQPTIYHLEK
     ADKLRVILYS TDFEHTVRDN RKVTYEIDLS QSKLIIPIES VKN