PEPX_LACDB
ID PEPX_LACDB Reviewed; 792 AA.
AC Q049K4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=LBUL_1351;
OS Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC BAA-365 / Lb-18).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=321956;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-365 / Lb-18;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000412; ABJ58868.1; -; Genomic_DNA.
DR RefSeq; WP_003618390.1; NC_008529.1.
DR AlphaFoldDB; Q049K4; -.
DR SMR; Q049K4; -.
DR ESTHER; lacdl-pepx; Lactobacillus_peptidase.
DR MEROPS; S15.001; -.
DR KEGG; lbu:LBUL_1351; -.
DR HOGENOM; CLU_011800_0_0_9; -.
DR OMA; LYTASPY; -.
DR BioCyc; LDEL321956:LBUL_RS06370-MON; -.
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..792
FT /note="Xaa-Pro dipeptidyl-peptidase"
FT /id="PRO_1000045481"
FT ACT_SITE 363
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT ACT_SITE 482
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT ACT_SITE 513
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
SQ SEQUENCE 792 AA; 88454 MW; F262BC19FF4ED364 CRC64;
MKYNQYAYVE TSPEKATEEL LAINFLPENY SSLSFSELLA VLTGNVLAEA TTRQAKDAKL
AEFAVDDQTD LAAFLLDTPT AITASQFANV ALQLLGYHPN YDYSLTDPLT CGEKHALPAF
KDLTSKEELI FAFYRLLNTR SKNGQILLDV MAGKGYFTQF WGEGKFMLFN GKSLPVFDTS
QVIREVVYVQ SDLDTDGDGK GDLLPVTIFR PVESQDQLKV PALYTASPYF GGIIDNVKTN
HNVDENLTDA TTWTNPKYVA KPLVKSPAPS GQDVPATELA TGQSSYGLNE YLLARGFASV
FSGAIGNRHG DGIRITGSPE ETISQKEVIE WLTGDRVAYT DRTRRFETKA SWCSGNVGMT
GRSYLGTLQI AIATTGVKGL KTVVSEAAIS SWYDYYREHG LVIAPSECQG EDMDKLAEVC
QSNLWDGGNF TAKKAYEAEQ AELLAAQDRA TGQYSDFWES RNYRHHADGI KCSWISVHGL
NDWNVKPKNV YKIWQKVKQL PVESHLFLHQ GPHYNMNNLV SIDFTDLMNL WFVHELLEVE
NGAYEQWPKV MIQDNLEADK WHAESDWAND LGQASLYSPT ADGYLSTVEN GTGQLTFTDL
GGTEFKKAGI SETDWEYQFI SGEKKWAKAS LRFESEEFLH PTTLVGRPKV QVRVAANKTV
GQLSVALVDL GTRQRLTATP KIFARGNQPF GYRFEADSLQ EFVPDKATKA KLITKAHMNL
QNYQDMKQPS KLEAGQFVDL EFELQPTYYT LPAGAKLCLI IYSTDQGMTK RPLETEDYTV
DLAGTALLLY RK