ID   PYRR_STRA3              Reviewed;         173 AA.
AC   Q8E4G7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Bifunctional protein PyrR {ECO:0000255|HAMAP-Rule:MF_01219};
DE   Includes:
DE     RecName: Full=Pyrimidine operon regulatory protein {ECO:0000255|HAMAP-Rule:MF_01219};
DE   Includes:
DE     RecName: Full=Uracil phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01219};
DE              Short=UPRTase {ECO:0000255|HAMAP-Rule:MF_01219};
DE              EC=2.4.2.9 {ECO:0000255|HAMAP-Rule:MF_01219};
GN   Name=pyrR {ECO:0000255|HAMAP-Rule:MF_01219}; OrderedLocusNames=gbs1434;
OS   Streptococcus agalactiae serotype III (strain NEM316).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=211110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEM316;
RX   PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA   Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA   Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT   "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT   neonatal disease.";
RL   Mol. Microbiol. 45:1499-1513(2002).
CC   -!- FUNCTION: Regulates transcriptional attenuation of the pyrimidine
CC       nucleotide (pyr) operon by binding in a uridine-dependent manner to
CC       specific sites on pyr mRNA. This disrupts an antiterminator hairpin in
CC       the RNA and favors formation of a downstream transcription terminator,
CC       leading to a reduced expression of downstream genes.
CC       {ECO:0000255|HAMAP-Rule:MF_01219}.
CC   -!- FUNCTION: Also displays a weak uracil phosphoribosyltransferase
CC       activity which is not physiologically significant. {ECO:0000255|HAMAP-
CC       Rule:MF_01219}.
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:0000255|HAMAP-Rule:MF_01219};
CC   -!- SUBUNIT: Homodimer and homohexamer; in equilibrium. {ECO:0000255|HAMAP-
CC       Rule:MF_01219}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. PyrR subfamily. {ECO:0000255|HAMAP-Rule:MF_01219}.
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DR   EMBL; AL766850; CAD47093.1; -; Genomic_DNA.
DR   RefSeq; WP_000823056.1; NC_004368.1.
DR   AlphaFoldDB; Q8E4G7; -.
DR   SMR; Q8E4G7; -.
DR   STRING; 211110.gbs1434; -.
DR   EnsemblBacteria; CAD47093; CAD47093; CAD47093.
DR   GeneID; 66886230; -.
DR   KEGG; san:gbs1434; -.
DR   eggNOG; COG2065; Bacteria.
DR   HOGENOM; CLU_094234_2_1_9; -.
DR   OMA; PIQPDFC; -.
DR   Proteomes; UP000000823; 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; RNA-binding; Transcription; Transcription regulation;
KW   Transcription termination; Transferase.
FT   CHAIN           1..173
FT                   /note="Bifunctional protein PyrR"
FT                   /id="PRO_1000053866"
FT   MOTIF           93..105
FT                   /note="PRPP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01219"
SQ   SEQUENCE   173 AA;  19800 MW;  9994B31C3F370B5D CRC64;
     MKRKEIIDDV TMKRAITRIT YEIIERNKNL DNIVLAGIKT RGVFLAKRIQ ERLKQLENLD
     IPVGELDTKP FRDDMKVEVD TTTMPVDITD KDIILIDDVL YTGRTIRAAI DNLVSLGRPS
     RVSLAVLIDR GHRELPIRAD YVGKNIPTSQ FEEILVEVME HDGYDRVSII DPS