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PYRR2_LACPL
ID   PYRR2_LACPL             Reviewed;         174 AA.
AC   P59389; F9UPD0;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   25-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Bifunctional protein PyrR 2;
DE   Includes:
DE     RecName: Full=Pyrimidine operon regulatory protein 2;
DE   Includes:
DE     RecName: Full=Uracil phosphoribosyltransferase 2;
DE              Short=UPRTase 2;
DE              EC=2.4.2.9;
GN   Name=pyrR2; OrderedLocusNames=lp_1782;
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 [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   [2]
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 (By similarity).
CC       {ECO:0000250}.
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}.
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DR   EMBL; AL935263; CCC79069.1; -; Genomic_DNA.
DR   RefSeq; WP_003644388.1; NC_004567.2.
DR   RefSeq; YP_004889583.1; NC_004567.2.
DR   AlphaFoldDB; P59389; -.
DR   SMR; P59389; -.
DR   STRING; 220668.lp_1782; -.
DR   EnsemblBacteria; CCC79069; CCC79069; lp_1782.
DR   GeneID; 57025395; -.
DR   KEGG; lpl:lp_1782; -.
DR   PATRIC; fig|220668.9.peg.1503; -.
DR   eggNOG; COG2065; Bacteria.
DR   HOGENOM; CLU_094234_2_1_9; -.
DR   OMA; VRITYEI; -.
DR   PhylomeDB; P59389; -.
DR   BioCyc; LPLA220668:G1GW0-1532-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..174
FT                   /note="Bifunctional protein PyrR 2"
FT                   /id="PRO_0000183042"
FT   MOTIF           96..108
FT                   /note="PRPP-binding"
FT                   /evidence="ECO:0000250"
FT   BINDING         39..40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         100..108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   174 AA;  19303 MW;  0547E7286C395B41 CRC64;
     MQKEVVDSMA MKRALTRITY EIIEQNKGIK NVVLVGVKTR GVYIAQRIAA QLQQLEGTAI
     PVGELDITAF RDDQPLDQAR LSTDYQLTFS VADKRVILVD DVLFTGRTIR AALDALMGGG
     RPQSIALAVL VDRGHRELPI RADFIGRNIP TARQERIKVT VNEIDGHDGI EIIN
 
 
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