ID   PYRR_THET2              Reviewed;         181 AA.
AC   Q72KT9;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Bifunctional protein PyrR;
DE   Includes:
DE     RecName: Full=Pyrimidine operon regulatory protein;
DE   Includes:
DE     RecName: Full=Uracil phosphoribosyltransferase;
DE              Short=UPRTase;
DE              EC=2.4.2.9;
GN   Name=pyrR; OrderedLocusNames=TT_C0428;
OS   Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=262724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX   PubMed=15064768; DOI=10.1038/nbt956;
RA   Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA   Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA   Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA   Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT   "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL   Nat. Biotechnol. 22:547-553(2004).
CC   -!- FUNCTION: Probably regulates transcriptional attenuation of the
CC       pyrimidine nucleotide (pyr) operon in response to exogenous
CC       pyrimidines. In contrast to pyr attenuation in Bacillus, PyrR from
CC       Thermus could act as a translational repressor: the binding of PyrR at
CC       its proposed recognition site in the transcript would prevent
CC       initiation of translation of the leader peptide, resulting in
CC       terminator formation and reduced expression of downstream genes (By
CC       similarity). Also displays uracil phosphoribosyltransferase activity
CC       (By similarity). {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   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. PyrR subfamily. {ECO:0000305}.
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DR   EMBL; AE017221; AAS80776.1; -; Genomic_DNA.
DR   RefSeq; WP_011172875.1; NC_005835.1.
DR   AlphaFoldDB; Q72KT9; -.
DR   SMR; Q72KT9; -.
DR   STRING; 262724.TT_C0428; -.
DR   EnsemblBacteria; AAS80776; AAS80776; TT_C0428.
DR   GeneID; 3169141; -.
DR   KEGG; tth:TT_C0428; -.
DR   eggNOG; COG2065; Bacteria.
DR   HOGENOM; CLU_094234_2_1_0; -.
DR   OMA; PIQPDFC; -.
DR   OrthoDB; 1725260at2; -.
DR   Proteomes; UP000000592; Chromosome.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; 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; Repressor; RNA-binding; Transcription;
KW   Transcription regulation; Transcription termination; Transferase.
FT   CHAIN           1..181
FT                   /note="Bifunctional protein PyrR"
FT                   /id="PRO_0000294121"
FT   MOTIF           99..111
FT                   /note="PRPP-binding"
FT                   /evidence="ECO:0000250"
FT   BINDING         41..42
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         82
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   BINDING         86
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         103..111
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         160
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   181 AA;  20467 MW;  87FDF462E6E6D3C9 CRC64;
     MRFKAELMNA PEMRRALYRI AHEIVEANKG TEGLALVGIH TRGIPLAHRI ARFIAEFEGK
     EVPVGVLDIT LYRDDLTEIG YRPQVRETRI PFDLTGKAIV LVDDVLYTGR TARAALDALI
     DLGRPRRIYL AVLVDRGHRE LPIRADFVGK NVPTSRSEVV KVKVEEVDGE DRVELWEREG
     A