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PYRR_ENTFA
ID   PYRR_ENTFA              Reviewed;         178 AA.
AC   P0DH77; O07659; O52707;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Bifunctional protein pyrR;
DE   Includes:
DE     RecName: Full=Pyrimidine operon regulatory protein;
DE   Includes:
DE     RecName: Full=Uracil phosphoribosyltransferase;
DE              Short=UPRTase;
DE              EC=2.4.2.9;
GN   Name=pyrR; OrderedLocusNames=EF_1721;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA   Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA   DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA   Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA   Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(2003).
CC   -!- FUNCTION: Regulates transcriptional attenuation of the pyrimidine
CC       nucleotide (pyr) operon in response to exogenous pyrimidines, by
CC       binding to the anti-antiterminator region of the 5' leader on pyr mRNA.
CC       This probably favors formation of a transcription terminator hairpin,
CC       leading to a reduced expression of downstream genes (By similarity).
CC       {ECO:0000250}.
CC   -!- FUNCTION: Also displays a weak uracil phosphoribosyltransferase
CC       activity which is not physiologically significant. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC         uracil; Xref=Rhea:RHEA:13017, ChEBI:CHEBI:17568, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57865, ChEBI:CHEBI:58017; EC=2.4.2.9;
CC   -!- SUBUNIT: Homodimer and homohexamer; in equilibrium. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. PyrR subfamily. {ECO:0000305}.
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DR   EMBL; AE016830; AAO81497.1; -; Genomic_DNA.
DR   RefSeq; NP_815427.1; NC_004668.1.
DR   RefSeq; WP_002357409.1; NZ_KE136528.1.
DR   AlphaFoldDB; P0DH77; -.
DR   SMR; P0DH77; -.
DR   STRING; 226185.EF_1721; -.
DR   EnsemblBacteria; AAO81497; AAO81497; EF_1721.
DR   GeneID; 60894017; -.
DR   KEGG; efa:EF1721; -.
DR   PATRIC; fig|226185.45.peg.1791; -.
DR   eggNOG; COG2065; Bacteria.
DR   HOGENOM; CLU_094234_2_1_9; -.
DR   OMA; PIQPDFC; -.
DR   Proteomes; UP000001415; Chromosome.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-UniRule.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   HAMAP; MF_01219; PyrR; 1.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR023050; PyrR.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; SSF53271; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Reference proteome; RNA-binding; Transcription;
KW   Transcription regulation; Transcription termination; Transferase.
FT   CHAIN           1..178
FT                   /note="Bifunctional protein pyrR"
FT                   /id="PRO_0000183035"
FT   MOTIF           97..109
FT                   /note="PRPP-binding"
FT                   /evidence="ECO:0000250"
FT   BINDING         40..41
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         101..109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   178 AA;  20139 MW;  FB6463307367ADDF CRC64;
     MPKKEVVDAV TMKRALTRIS YEIIERNKGI QDIVLVGIKT RGIYIAQRLA ERLKQLEDID
     VPVGELDITL YRDDVKDMEE PELHSSDVPV SIEGKEVILV DDVLYTGRTI RAAMDAVMDL
     GRPRKISLAV LVDRGHRELP IRADYVGKNI PTSKTEEIIV EMEERDGADR IMISKGNE
 
 
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