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