PYRR1_LACPL
ID PYRR1_LACPL Reviewed; 180 AA.
AC P71479; F9URI6;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Bifunctional protein PyrR 1;
DE Includes:
DE RecName: Full=Pyrimidine operon regulatory protein 1;
DE Includes:
DE RecName: Full=Uracil phosphoribosyltransferase 1;
DE Short=UPRTase 1;
DE EC=2.4.2.9;
GN Name=pyrR1; Synonyms=pyrR; OrderedLocusNames=lp_2704;
OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS (Lactobacillus plantarum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=220668;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 8014 / CCM 1904 / DSM 20205 / NCDO 82 / NCIB 6376;
RX PubMed=8982065; DOI=10.1016/s0378-1119(96)00461-1;
RA Elagoez A., Abdi A., Hubert J.-C., Kammerer B.;
RT "Structure and organisation of the pyrimidine biosynthesis pathway genes in
RT Lactobacillus plantarum: a PCR strategy for sequencing without cloning.";
RL Gene 182:37-43(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA Siezen R.J.;
RT "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=22156394; DOI=10.1128/jb.06275-11;
RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA Kleerebezem M., van Hijum S.A.;
RT "Complete resequencing and reannotation of the Lactobacillus plantarum
RT WCFS1 genome.";
RL J. Bacteriol. 194:195-196(2012).
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 (Probable).
CC {ECO:0000305}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z54240; CAA91001.1; -; Genomic_DNA.
DR EMBL; AL935263; CCC79825.1; -; Genomic_DNA.
DR RefSeq; WP_003639428.1; NC_004567.2.
DR RefSeq; YP_004890339.1; NC_004567.2.
DR AlphaFoldDB; P71479; -.
DR SMR; P71479; -.
DR STRING; 220668.lp_2704; -.
DR EnsemblBacteria; CCC79825; CCC79825; lp_2704.
DR GeneID; 49394818; -.
DR GeneID; 57026085; -.
DR GeneID; 66450362; -.
DR KEGG; lpl:lp_2704; -.
DR PATRIC; fig|220668.9.peg.2264; -.
DR eggNOG; COG2065; Bacteria.
DR HOGENOM; CLU_094234_2_1_9; -.
DR OMA; PVSANYV; -.
DR PhylomeDB; P71479; -.
DR BioCyc; LPLA220668:G1GW0-2316-MON; -.
DR Proteomes; UP000000432; 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..180
FT /note="Bifunctional protein PyrR 1"
FT /id="PRO_0000183041"
FT MOTIF 99..111
FT /note="PRPP-binding"
FT /evidence="ECO:0000250"
FT BINDING 39..40
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 103..111
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 180 AA; 19824 MW; 5ADBBFA61AA3172D CRC64;
MAREVVDAMT MRRALTRITY EIIEQNKGVG NLVFIGIKTR GIFLAQRLAQ RLKQLEGVDV
PVGSLDITLY RDDHHAVDVA GQAKLNGADI PVDINGKHVI LVDDVLFTGR TVRAALDALM
DHGRPAKISL AVLVDRGHRE LPIRPDFIGK NIPTALDEQV SVALEEHDGH DGISIEKLEE
