PYRR_ENTFO
ID PYRR_ENTFO Reviewed; 178 AA.
AC F2MMP6; O07659; O52707;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-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=OG1RF_11432;
OS Enterococcus faecalis (strain ATCC 47077 / OG1RF).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=474186;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 47077 / OG1RF;
RX PubMed=9973361; DOI=10.1128/jb.181.4.1324-1329.1999;
RA Ghim S.-Y., Kim C.C., Bonner E.R., D'Elia J.N., Grabner G.K., Switzer R.L.;
RT "The Enterococcus faecalis pyr operon is regulated by autogenous
RT transcriptional attenuation at a single site in the 5' leader.";
RL J. Bacteriol. 181:1324-1329(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47077 / OG1RF;
RX PubMed=18611278; DOI=10.1186/gb-2008-9-7-r110;
RA Bourgogne A., Garsin D.A., Qin X., Singh K.V., Sillanpaa J.,
RA Yerrapragada S., Ding Y., Dugan-Rocha S., Buhay C., Shen H., Chen G.,
RA Williams G., Muzny D., Maadani A., Fox K.A., Gioia J., Chen L., Shang Y.,
RA Arias C.A., Nallapareddy S.R., Zhao M., Prakash V.P., Chowdhury S.,
RA Jiang H., Gibbs R.A., Murray B.E., Highlander S.K., Weinstock G.M.;
RT "Large scale variation in Enterococcus faecalis illustrated by the genome
RT analysis of strain OG1RF.";
RL Genome Biol. 9:R110.1-R110.16(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-101.
RC STRAIN=ATCC 47077 / OG1RF;
RX PubMed=7592480; DOI=10.1128/jb.177.23.6866-6873.1995;
RA Li X., Weinstock G.M., Murray B.E.;
RT "Generation of auxotrophic mutants of Enterococcus faecalis.";
RL J. Bacteriol. 177:6866-6873(1995).
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.
CC {ECO:0000269|PubMed:9973361}.
CC -!- FUNCTION: Also displays a weak uracil phosphoribosyltransferase
CC activity which is not physiologically significant.
CC {ECO:0000269|PubMed:9973361}.
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 Evidence={ECO:0000269|PubMed:9973361};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9.2 for UPRTase activity. {ECO:0000269|PubMed:9973361};
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; AF044978; AAC12929.1; -; Genomic_DNA.
DR EMBL; CP002621; AEA94119.1; -; Genomic_DNA.
DR EMBL; U25091; AAB61217.1; -; Genomic_DNA.
DR RefSeq; WP_002357409.1; NZ_CP025020.1.
DR AlphaFoldDB; F2MMP6; -.
DR SMR; F2MMP6; -.
DR GeneID; 60894017; -.
DR KEGG; efi:OG1RF_11432; -.
DR HOGENOM; CLU_094234_2_1_9; -.
DR OMA; PIQPDFC; -.
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 1: Evidence at protein level;
KW Glycosyltransferase; RNA-binding; Transcription; Transcription regulation;
KW Transcription termination; Transferase.
FT CHAIN 1..178
FT /note="Bifunctional protein pyrR"
FT /id="PRO_0000412181"
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"
FT CONFLICT 100..101
FT /note="VD -> GG (in Ref. 3; AAB61217)"
FT /evidence="ECO:0000305"
FT CONFLICT 132..133
FT /note="VD -> AA (in Ref. 1; AAC12929)"
FT /evidence="ECO:0000305"
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
