PYRR_LACLM
ID PYRR_LACLM Reviewed; 173 AA.
AC Q9L4N8; A2RJN2;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Pyrimidine operon regulatory protein;
GN Name=pyrR; OrderedLocusNames=llmg_0890;
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11292797; DOI=10.1128/jb.183.9.2785-2794.2001;
RA Martinussen J., Schallert J., Andersen B., Hammer K.;
RT "The pyrimidine operon pyrRPB-carA from Lactococcus lactis.";
RL J. Bacteriol. 183:2785-2794(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363;
RX PubMed=17307855; DOI=10.1128/jb.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
CC -!- FUNCTION: Regulates transcriptional attenuation of the pyrimidine
CC nucleotide (pyr) operon in response to exogenous pyrimidines, probably
CC by binding to specific sites on pyr mRNA. This probably disrupts an
CC antiterminator hairpin in the RNA and favors formation of a downstream
CC transcription terminator, leading to a reduced expression of downstream
CC genes.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. PyrR subfamily. {ECO:0000305}.
CC -!- CAUTION: Unlike for B.subtilis, the PyrR protein of L.lactis was shown
CC not to encode UPRTase activity. {ECO:0000305}.
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DR EMBL; AJ132624; CAB89869.1; -; Genomic_DNA.
DR EMBL; AM406671; CAL97485.1; -; Genomic_DNA.
DR RefSeq; WP_011676642.1; NZ_WJVF01000036.1.
DR AlphaFoldDB; Q9L4N8; -.
DR SMR; Q9L4N8; -.
DR STRING; 416870.llmg_0890; -.
DR EnsemblBacteria; CAL97485; CAL97485; llmg_0890.
DR GeneID; 61109848; -.
DR KEGG; llm:llmg_0890; -.
DR eggNOG; COG2065; Bacteria.
DR HOGENOM; CLU_094234_2_1_9; -.
DR OMA; PIQPDFC; -.
DR PhylomeDB; Q9L4N8; -.
DR BioCyc; LLAC416870:LLMG_RS04550-MON; -.
DR Proteomes; UP000000364; 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 RNA-binding; Transcription; Transcription regulation;
KW Transcription termination.
FT CHAIN 1..173
FT /note="Pyrimidine operon regulatory protein"
FT /id="PRO_0000183040"
FT MOTIF 93..105
FT /note="PRPP-binding"
FT /evidence="ECO:0000250"
FT BINDING 40..41
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 97..105
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 173 AA; 19812 MW; C13917C1E9E5877E CRC64;
MARKEIIDEI TMKRAITRIT YEIIERNKEL DKLVLIGIKT RGVYLAKRIQ ERLQQLEGLE
IPFGELDTRP FRDDKQAQED TTEIDIDITG KDVILVDDVL YTGRTIRAAI DGIVKLGRPA
RVQLAVLVDR GHRELPIRAD YVGKNIPTGH DEEIIVQMSE HDGNDSILIK RED