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Database: UniProt
Entry: D2BKP0_LACLK
LinkDB: D2BKP0_LACLK
Original site: D2BKP0_LACLK 
ID   D2BKP0_LACLK            Unreviewed;       173 AA.
AC   D2BKP0;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   24-JAN-2024, entry version 81.
DE   RecName: Full=Bifunctional protein PyrR {ECO:0000256|HAMAP-Rule:MF_01219};
DE   Includes:
DE     RecName: Full=Pyrimidine operon regulatory protein {ECO:0000256|HAMAP-Rule:MF_01219};
DE   Includes:
DE     RecName: Full=Uracil phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01219};
DE              Short=UPRTase {ECO:0000256|HAMAP-Rule:MF_01219};
DE              EC=2.4.2.9 {ECO:0000256|HAMAP-Rule:MF_01219};
GN   Name=pyrR {ECO:0000256|HAMAP-Rule:MF_01219,
GN   ECO:0000313|EMBL:ADA65346.1};
GN   OrderedLocusNames=LLKF_1756 {ECO:0000313|EMBL:ADA65346.1};
OS   Lactococcus lactis subsp. lactis (strain KF147).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=684738 {ECO:0000313|EMBL:ADA65346.1, ECO:0000313|Proteomes:UP000001886};
RN   [1] {ECO:0000313|EMBL:ADA65346.1, ECO:0000313|Proteomes:UP000001886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KF147 {ECO:0000313|EMBL:ADA65346.1,
RC   ECO:0000313|Proteomes:UP000001886};
RX   PubMed=18039825; DOI=10.1128/AEM.01850-07;
RA   Siezen R.J., Starrenburg M.J., Boekhorst J., Renckens B., Molenaar D.,
RA   van Hylckama Vlieg J.E.;
RT   "Genome-scale genotype-phenotype matching of two Lactococcus lactis
RT   isolates from plants identifies mechanisms of adaptation to the plant
RT   niche.";
RL   Appl. Environ. Microbiol. 74:424-436(2008).
CC   -!- FUNCTION: Also displays a weak uracil phosphoribosyltransferase
CC       activity which is not physiologically significant. {ECO:0000256|HAMAP-
CC       Rule:MF_01219}.
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:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_01219};
CC   -!- SUBUNIT: Homodimer and homohexamer; in equilibrium. {ECO:0000256|HAMAP-
CC       Rule:MF_01219}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. PyrR subfamily. {ECO:0000256|ARBA:ARBA00005565,
CC       ECO:0000256|HAMAP-Rule:MF_01219}.
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DR   EMBL; CP001834; ADA65346.1; -; Genomic_DNA.
DR   RefSeq; WP_010906054.1; NC_013656.1.
DR   AlphaFoldDB; D2BKP0; -.
DR   SMR; D2BKP0; -.
DR   GeneID; 69713684; -.
DR   KEGG; llk:LLKF_1756; -.
DR   HOGENOM; CLU_094234_2_1_9; -.
DR   OMA; PIQPDFC; -.
DR   Proteomes; UP000001886; 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   PANTHER; PTHR11608; BIFUNCTIONAL PROTEIN PYRR; 1.
DR   PANTHER; PTHR11608:SF0; BIFUNCTIONAL PROTEIN PYRR; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01219,
KW   ECO:0000313|EMBL:ADA65346.1};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01219};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_01219};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW   Rule:MF_01219};
KW   Transcription termination {ECO:0000256|ARBA:ARBA00022472,
KW   ECO:0000256|HAMAP-Rule:MF_01219};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01219, ECO:0000313|EMBL:ADA65346.1}.
FT   DOMAIN          9..158
FT                   /note="Phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00156"
FT   MOTIF           93..105
FT                   /note="PRPP-binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01219"
SQ   SEQUENCE   173 AA;  19831 MW;  608317C1E9E5876E CRC64;
     MARKEIIDEI TMKRAITRIT YEIIERNKEL DKLVLIGIKT RGVYLAKRIQ ERLQQLEGLE
     IPFGELDTRP FRDDKQAQED TTEIDIDITG KDVILVDDVL YTGRTIRAAI DGIVKLGRPA
     RVQLAVLVDR GHRELPIRAD YVGKNIPTGR DEEIIVQMSE HDGNDSILIK RED
//
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