PEPX_LACPL
ID PEPX_LACPL Reviewed; 813 AA.
AC Q88YC0; F9UM69;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=lp_0857;
OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS (Lactobacillus plantarum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=220668;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA Siezen R.J.;
RT "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=22156394; DOI=10.1128/jb.06275-11;
RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA Kleerebezem M., van Hijum S.A.;
RT "Complete resequencing and reannotation of the Lactobacillus plantarum
RT WCFS1 genome.";
RL J. Bacteriol. 194:195-196(2012).
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; AL935263; CCC78308.1; -; Genomic_DNA.
DR RefSeq; WP_011101183.1; NC_004567.2.
DR RefSeq; YP_004888822.1; NC_004567.2.
DR AlphaFoldDB; Q88YC0; -.
DR SMR; Q88YC0; -.
DR STRING; 220668.lp_0857; -.
DR ESTHER; lacpl-pepx; Lactobacillus_peptidase.
DR EnsemblBacteria; CCC78308; CCC78308; lp_0857.
DR GeneID; 57024549; -.
DR KEGG; lpl:lp_0857; -.
DR PATRIC; fig|220668.9.peg.728; -.
DR eggNOG; COG2936; Bacteria.
DR HOGENOM; CLU_011800_0_0_9; -.
DR OMA; LYTASPY; -.
DR PhylomeDB; Q88YC0; -.
DR BioCyc; LPLA220668:G1GW0-744-MON; -.
DR Proteomes; UP000000432; 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..813
FT /note="Xaa-Pro dipeptidyl-peptidase"
FT /id="PRO_0000220222"
FT ACT_SITE 375
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT ACT_SITE 495
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT ACT_SITE 526
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
SQ SEQUENCE 813 AA; 91548 MW; FBA685F68C0119BB CRC64;
MKNNQFAIVP TDSETAIAEL TKIHFITPDM DALTTVPAVY QALLAKSLPE VHTASGLTHK
FNNIMATSQH TLSEWLADAT IVNNQVFYNV GLQLLGFLPG QDFELADPLL AMRDIHLPMV
GDSAFDREAL YYAWYLLLNT RGNNGQTLIE SLTTRGYFVP FYQLPNDQKP LFFNGKAQAV
FDTNALIRDV VYVEAPLDTD HDGQRDLLKV EILRPAETET GLKVPVLYTA SPYNQGINDQ
AGDAQMHNVD VPLTAKEPDE NTYADVEFQP TTAQLPAART ATTTTDTAEE TFSREKSYTL
NDYFLARGFA VVYAAGIGSI DSDGLAPTGD VDETTSTVAI IEWLTGKRQA FTNRDGNIAI
KAWWCNGAVA MTGRSYLGTL ATAAATTGVA GLKTIISEAA ISSWYDYYRD NGLVVAPDTF
QGEDTDVLAA EVFSRSLKAG DAHQIQPAFD QKLAELTADQ DRASGNYNRF WDERNYLKNV
DKIKADIIMV HGLNDWNVKP RNVANLWDKL QAVPVTKKLI LHQGQHIYIN NLQSLDFTDM
MNLWLSHKLY GLDNHAETLL PNVLVQDNTQ AQTWHGYDNW WQDTTDALDF KVQYKELVPA
DHTVDQRAAH FTDKLPDKLF DHYKHHLDSW QRDLLQEDKL NPLYDHRLLF KSWQAPEDQL
LVGIPHVAGS VAVNKNFGML SFMLIDFGAA RRLTVSPQIL AAKALDLGYH WREDDLKDFK
LAGETPFKMI TKGHLNLQNR HHPWHAEAIQ PNVFYDFSVD LQPLFHHLLK GHQLGLVIYA
TDMKMTIRGN QDLQYSLNLN DIRLHVPMKK ITD
