ID   PYRR_STRMU              Reviewed;         176 AA.
AC   Q8DUP7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 117.
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=SMU_856;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(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; AE014133; AAN58572.1; -; Genomic_DNA.
DR   RefSeq; NP_721266.1; NC_004350.2.
DR   RefSeq; WP_002262005.1; NC_004350.2.
DR   AlphaFoldDB; Q8DUP7; -.
DR   SMR; Q8DUP7; -.
DR   STRING; 210007.SMU_856; -.
DR   PRIDE; Q8DUP7; -.
DR   EnsemblBacteria; AAN58572; AAN58572; SMU_856.
DR   GeneID; 66817708; -.
DR   KEGG; smu:SMU_856; -.
DR   PATRIC; fig|210007.7.peg.763; -.
DR   eggNOG; COG2065; Bacteria.
DR   HOGENOM; CLU_094234_2_1_9; -.
DR   OMA; PIQPDFC; -.
DR   PhylomeDB; Q8DUP7; -.
DR   Proteomes; UP000002512; 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..176
FT                   /note="Bifunctional protein PyrR"
FT                   /id="PRO_1000053868"
FT   MOTIF           93..105
FT                   /note="PRPP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01219"
SQ   SEQUENCE   176 AA;  19870 MW;  335ECF18E0D54B11 CRC64;
     MKTKEIVDGV TMKRAITRMT YEIIERNKNL DNIVLAGIKT RGVFIARRIQ ERLKQIEGLD
     VPLGELDTKS FRDDVKVEEN TTEMPVDITN RDVILVDDVL YTGRTIRAAI DNIVNLGRPA
     RVSLAVLVDR GHRELPIRAD YVGKNIPTSS SEEIVVNMVE IDDKDNVLLL AKEDSL