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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}.
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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
 
 
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