ID   PYRR_LEUMM              Reviewed;         175 AA.
AC   Q03WF7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 86.
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=LEUM_1372;
OS   Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 / DSM
OS   20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523 / NBRC 100496 / NCIMB
OS   8023 / NCTC 12954 / NRRL B-1118 / 37Y).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Leuconostoc.
OX   NCBI_TaxID=203120;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8293 / DSM 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523
RC   / NBRC 100496 / NCIMB 8023 / NCTC 12954 / NRRL B-1118 / 37Y;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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; CP000414; ABJ62465.1; -; Genomic_DNA.
DR   RefSeq; WP_011680067.1; NC_008531.1.
DR   AlphaFoldDB; Q03WF7; -.
DR   SMR; Q03WF7; -.
DR   STRING; 203120.LEUM_1372; -.
DR   EnsemblBacteria; ABJ62465; ABJ62465; LEUM_1372.
DR   GeneID; 61176149; -.
DR   KEGG; lme:LEUM_1372; -.
DR   eggNOG; COG2065; Bacteria.
DR   HOGENOM; CLU_094234_2_1_9; -.
DR   OMA; PVSANYV; -.
DR   OrthoDB; 1725260at2; -.
DR   Proteomes; UP000000362; 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..175
FT                   /note="Bifunctional protein PyrR"
FT                   /id="PRO_1000053844"
FT   MOTIF           97..109
FT                   /note="PRPP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01219"
SQ   SEQUENCE   175 AA;  19719 MW;  5345B61DC770EB1B CRC64;
     MPNKEVLDNA SLQRALTRIT YEIIERNKGG KNLVLVGIKT RGEYLARRIA DRLEQLEGVQ
     IPVMAIDITN FRDDKPDQHN DLGLNSEERL NISEQNIVLI DDVLFTGRTI RAALDALIHI
     GRPKTISLAV LVDRGHRELP IRADFVGKNI PTAQNEKIKV FVQEIDGKDA VEIVH