ID   PEPX_LACCB              Reviewed;         797 AA.
AC   B3WEZ5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=LCABL_18670;
OS   Lacticaseibacillus casei (strain BL23) (Lactobacillus casei).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=543734;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL23;
RA   Maze A., Boel G., Bourand A., Loux V., Gibrat J.F., Zuniga M., Hartke A.,
RA   Deutscher J.;
RT   "Lactobacillus casei BL23 complete genome sequence.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; FM177140; CAQ66946.1; -; Genomic_DNA.
DR   RefSeq; WP_012491657.1; NC_010999.1.
DR   AlphaFoldDB; B3WEZ5; -.
DR   SMR; B3WEZ5; -.
DR   ESTHER; lacc3-pepx; Lactobacillus_peptidase.
DR   MEROPS; S15.001; -.
DR   KEGG; lcb:LCABL_18670; -.
DR   HOGENOM; CLU_011800_0_0_9; -.
DR   OMA; LYTASPY; -.
DR   OrthoDB; 327988at2; -.
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..797
FT                   /note="Xaa-Pro dipeptidyl-peptidase"
FT                   /id="PRO_1000132340"
FT   ACT_SITE        370
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT   ACT_SITE        490
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT   ACT_SITE        521
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
SQ   SEQUENCE   797 AA;  88434 MW;  8561A80689D18A74 CRC64;
     MKLNQFARLT PDFKVQVAEL KQIGLQADPD DAFSQSATDL FNAFFPEAYT LAAKEDKLAQ
     VAVNMDQTLA AWLAKKPSKM TRRDFYNVAL QLLGFEAFTD FDLNDPFKMM TATKLPSLDH
     DLTSTADLLK AVYLLLNTRT KHLVSYLDDL ANRGFLKDFQ KKQKKPTHLL FNGKVQQVFD
     ARQAVREVVW IESDMDTDHD GQRDLLEATI YRPKATDQGL KVPVLFTANP YFHGTNDVTA
     VTHVPETTLA VKTHGASKAE VTANPEEPAN LPHHPVNGEA TQAEAYAEEN SMYAFNDYFL
     ARGFAVVYSA GVGTRYSDGF RTTGGPEETD GAVAVIEWLT GKRRAFTNRT DGITIKAWWS
     TGLVAMTGKS YLATLAMAAA TTGVDGLKTI VADAGISSWY DYYRENGLVV APGGFQGEDA
     DVLAVDTFSR QKSGGDLINI KQAWEKHLAT ITHDQDRTTG AYNTWWDARN YRKNANKVKA
     DVVLIHGLND WNVKPTNAIK FWEAIADLPI QKKLVLHQGQ HVYVHNVRSL DFLDMMNLWL
     THELLGEANG AEDVLPNVVV QDNVAVQTWS AYQNFASPAA EHVTNTRNLK TDFEAATDQF
     TDHATATFNA QHDTSASFET AIITPNSAYA NSRLWLTQPP LERDQTLEGI PHLELTLAID
     APTGILSVRL IDLGMAKRFG ETAATVALNG LQLGFDYKTT DILEFKPTAK PTPSKLISLG
     HINLQNPKNA YEVQRITPGQ PFHISLDLQP THYHLPAGRQ LALVIHGADM AQTIRPIKTT
     HYQIDLANSS ITLPYRI