位置:首页 > 蛋白库 > PEPX_STRP3
PEPX_STRP3
ID   PEPX_STRP3              Reviewed;         760 AA.
AC   P0DD36; Q8K5X7;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 53.
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}; Synonyms=pepXP;
GN   OrderedLocusNames=SpyM3_1603;
OS   Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=198466;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-595 / MGAS315;
RX   PubMed=12122206; DOI=10.1073/pnas.152298499;
RA   Beres S.B., Sylva G.L., Barbian K.D., Lei B., Hoff J.S., Mammarella N.D.,
RA   Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D., Campbell D.S.,
RA   Smith T.M., McCormick J.K., Leung D.Y.M., Schlievert P.M., Musser J.M.;
RT   "Genome sequence of a serotype M3 strain of group A Streptococcus: phage-
RT   encoded toxins, the high-virulence phenotype, and clone emergence.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(2002).
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; AE014074; AAM80210.1; -; Genomic_DNA.
DR   RefSeq; WP_011054979.1; NC_004070.1.
DR   AlphaFoldDB; P0DD36; -.
DR   SMR; P0DD36; -.
DR   EnsemblBacteria; AAM80210; AAM80210; SpyM3_1603.
DR   KEGG; spg:SpyM3_1603; -.
DR   HOGENOM; CLU_011800_0_0_9; -.
DR   OMA; LYTASPY; -.
DR   Proteomes; UP000000564; 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..760
FT                   /note="Xaa-Pro dipeptidyl-peptidase"
FT                   /id="PRO_0000220232"
FT   ACT_SITE        349
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT   ACT_SITE        469
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT   ACT_SITE        499
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
SQ   SEQUENCE   760 AA;  86719 MW;  B9F9119217A71ACD CRC64;
     MRYNQFSYIP TSLERAAEEL KELGFDLDLQ KTAKANLESF LRKLFFHYPD SDYPLSHLIA
     KNDMDALSFF QSEQELSKEV FDLLALQVLG FIPGVDFTEA DAFLDKLAFP IHFDETEIIK
     HIHHLLATRC KSGMTLIDDL VSQGMLTMDN DYHFFNGKSL ATFDTSQLIR EVVYVEAPLD
     TDQDGQLDLI KVNIIRPQSQ KPLPTLMTPS PYHQGINEVA NDKKLYRMEK ELVVKKRRQI
     TVEDRDFIPL ETQPCKLPIG QNLESFSYIN SYSLNDYFLA RGFANIYVSG VGTAGSTGFM
     TSGDYAQIES FKAVIDWLNG RATAYTSHSK THQVRADWAN GLVCTTGKSY LGTMSTGLAT
     TGVDGLAMII AESAISSWYN YYRENGLVCS PGGYPGEDLD VLTELTYSRN LLAGDYLRHN
     DRYQELLNQQ SQALDRQSGD YNQFWHDRNY LKNAHQIKCD VVYTHGLQDW NVKPRQVYEI
     VNALPSTINK HLFLHQGEHV YMHNWQSIDF RESMNALLCQ KLLGLANDFS LPEMIWQDNT
     CPQNWQERKV FGTSTIKELD LGQELLLIDN HYGEDEFKAY GKDFRAFKAA LFKGKANQAL
     VDILLEEDLL INGEIVLQLK VKSSENKGLL SAQILDYGKK KRLGDLPIAL TQSSIDNGQN
     FSREPLKELP FRENSYRVIS KGFMNLQNRN NLSSIETIPN NKWMTVRLPL QPTIYHLEKG
     DTLRVILYTT DFEHTVRDNS NYALTIDLSQ SQLIVPIASN
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024