ID   PEPX_LACH4              Reviewed;         793 AA.
AC   A8YVY9;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=lhv_1436;
OS   Lactobacillus helveticus (strain DPC 4571).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=405566;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DPC 4571;
RX   PubMed=17993529; DOI=10.1128/jb.01295-07;
RA   Callanan M., Kaleta P., O'Callaghan J., O'Sullivan O., Jordan K.,
RA   McAuliffe O., Sangrador-Vegas A., Slattery L., Fitzgerald G.F.,
RA   Beresford T., Ross R.P.;
RT   "Genome sequence of Lactobacillus helveticus: an organism distinguished by
RT   selective gene loss and IS element expansion.";
RL   J. Bacteriol. 190:727-735(2008).
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; CP000517; ABX27419.1; -; Genomic_DNA.
DR   RefSeq; WP_012212045.1; NC_010080.1.
DR   AlphaFoldDB; A8YVY9; -.
DR   SMR; A8YVY9; -.
DR   STRING; 405566.lhv_1436; -.
DR   ESTHER; lache-pepx; Lactobacillus_peptidase.
DR   MEROPS; S15.001; -.
DR   EnsemblBacteria; ABX27419; ABX27419; lhv_1436.
DR   KEGG; lhe:lhv_1436; -.
DR   eggNOG; COG2936; Bacteria.
DR   HOGENOM; CLU_011800_0_0_9; -.
DR   OMA; LYTASPY; -.
DR   Proteomes; UP000000790; 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..793
FT                   /note="Xaa-Pro dipeptidyl-peptidase"
FT                   /id="PRO_1000072762"
FT   ACT_SITE        363
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT   ACT_SITE        483
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT   ACT_SITE        514
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
SQ   SEQUENCE   793 AA;  90573 MW;  7646868E9A75A818 CRC64;
     MKYNQYAYVE TDFQQQVKEL IDINFLPKNY QVWDFSSLLA KLVKNAIAEA KTDAAKNAKL
     AEFAVSDHQT LADFLKEKPT EIGTEQFYNV ALQLLGYHVH YDYDFADPTG FMQRNALPFV
     QDISDNQKLI SAFYRLLNTR AKNGQILLDV MAGKGYFTQF WGQNKFKFFN GKSIPVFDTN
     KVIREVVYVE TDLDTDHDGK SDLIQVTVFR PEETNKGLKV PALYTASPYF GGIIANEKRN
     HNVDENLSDS TEWNDPQYVH SPIVKAEKPD GSSRPATEEA VHKSSYPLNE YMLARGFASV
     FAGAIGTRGS DGVRITGAPE ETESAAAVIE WLHGDRVAYT DRTRTVQTTA DWCNGNIGMT
     GRSYLGTLQI AIATTGVKGL KTVVSEAAIS SWYDYYREHG LVIAPEACQG EDLDLLAETC
     QSNLWDAGSY LKIKPEYDKM QKQLREKEDR NTGQYSDFWE ARNYRHHADG IKCSWISVHG
     LNDWNVKPKN VYKIWQLVKK MPMKHHLFLH QGPHYNMNNF VSIDFTDFMN LWFVHELLGI
     ENNAYNQWPT VMIQDNLQAD KWHEEPDWSN DLGQEKIYYP TDEGELFQDG NGKAQKSFTD
     VGGIEFKKAG ISESDWQYKF ICGDEKWAKP SLRFETDEFI HPTTIVGRPE VKVRVSASLP
     KGEISVALVE LGERQRLTAT PKFLMRGGQE LGYRFGTDTL QEFVPDKKTK AKLITKAHMN
     LQNFKDMKKP EAIDADKFYD LDFLLQPTYY TIPSGSKLAL IIYSTDQGMT KRPLEDETYT
     IDLANTEIKF YEK