PYRR_STRPN
ID PYRR_STRPN Reviewed; 173 AA.
AC P65946; Q97QE1;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=SP_1278;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
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 -!- INTERACTION:
CC P65946; P63544: apt; NbExp=2; IntAct=EBI-2207248, EBI-2207316;
CC P65946; P95830: dnaJ; NbExp=2; IntAct=EBI-2207248, EBI-2207079;
CC P65946; Q97QS2: eno; NbExp=2; IntAct=EBI-2207248, EBI-2207206;
CC P65946; Q97SE5: gatC; NbExp=2; IntAct=EBI-2207248, EBI-2207053;
CC P65946; Q97NV3: groES; NbExp=2; IntAct=EBI-2207248, EBI-2206949;
CC P65946; Q9X9S0: pyrDA; NbExp=2; IntAct=EBI-2207248, EBI-2207999;
CC P65946; A0A0H2UPY3: SP_1103; NbExp=2; IntAct=EBI-2207248, EBI-2207193;
CC P65946; Q97SR4: uppS; NbExp=2; IntAct=EBI-2207248, EBI-2206983;
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. PyrR subfamily. {ECO:0000255|HAMAP-Rule:MF_01219}.
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DR EMBL; AE005672; AAK75382.1; -; Genomic_DNA.
DR PIR; E95148; E95148.
DR RefSeq; WP_000850024.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; P65946; -.
DR SMR; P65946; -.
DR IntAct; P65946; 8.
DR STRING; 170187.SP_1278; -.
DR EnsemblBacteria; AAK75382; AAK75382; SP_1278.
DR GeneID; 60233963; -.
DR GeneID; 66806388; -.
DR KEGG; spn:SP_1278; -.
DR eggNOG; COG2065; Bacteria.
DR OMA; PIQPDFC; -.
DR PhylomeDB; P65946; -.
DR BioCyc; SPNE170187:G1FZB-1291-MON; -.
DR PHI-base; PHI:8614; -.
DR Proteomes; UP000000585; 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 1: Evidence at protein level;
KW Glycosyltransferase; RNA-binding; Transcription; Transcription regulation;
KW Transcription termination; Transferase.
FT CHAIN 1..173
FT /note="Bifunctional protein PyrR"
FT /id="PRO_0000183064"
FT MOTIF 93..105
FT /note="PRPP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01219"
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; 19608 MW; FF2E445E1568CC47 CRC64;
MKTKEVVDEL TVKRAITRIT YEIIERNKDL NKIVLAGIKT RGVFIAHRIQ ERLKQLENLS
VPVVELDTKP FRDDVKSGED TSLVSVDVTD REVILVDDVL YTGRTIRAAI DNIVGHGRPA
RVSLAVLVDR GHRELPIRPD YVGKNIPTSR SEEIIVEMTE LDDQDRVLIT EEA
