ID   PYRR_BACCL              Reviewed;         179 AA.
AC   P41007;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 101.
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;
OS   Bacillus caldolyticus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=1394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 405 / NBRC 15313 / YP-T;
RX   PubMed=8206848; DOI=10.1128/jb.176.12.3698-3707.1994;
RA   Ghim S.Y., Neuhard J.;
RT   "The pyrimidine biosynthesis operon of the thermophile Bacillus
RT   caldolyticus includes genes for uracil phosphoribosyltransferase and uracil
RT   permease.";
RL   J. Bacteriol. 176:3698-3707(1994).
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 (Probable).
CC       {ECO:0000305}.
CC   -!- FUNCTION: Also displays a weak uracil phosphoribosyltransferase
CC       activity which is not physiologically significant.
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; X76083; CAA53696.1; -; Genomic_DNA.
DR   PIR; S38892; S38892.
DR   RefSeq; WP_011230647.1; NZ_CP025074.1.
DR   PDB; 1NON; X-ray; 2.40 A; A/B/C/D=1-179.
DR   PDB; 1XZ8; X-ray; 2.80 A; A/B=1-179.
DR   PDB; 1XZN; X-ray; 2.27 A; A/B=1-179.
DR   PDB; 2IGB; X-ray; 1.68 A; A/B=1-179.
DR   PDBsum; 1NON; -.
DR   PDBsum; 1XZ8; -.
DR   PDBsum; 1XZN; -.
DR   PDBsum; 2IGB; -.
DR   AlphaFoldDB; P41007; -.
DR   SMR; P41007; -.
DR   DrugBank; DB03315; Guanosine 3'-monophosphate.
DR   DrugBank; DB01972; Guanosine-5'-Monophosphate.
DR   DrugBank; DB03685; Uridine monophosphate.
DR   MoonProt; P41007; -.
DR   EvolutionaryTrace; P41007; -.
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   3D-structure; Glycosyltransferase; RNA-binding; Transcription;
KW   Transcription regulation; Transcription termination; Transferase.
FT   CHAIN           1..179
FT                   /note="Bifunctional protein PyrR"
FT                   /id="PRO_0000183028"
FT   MOTIF           100..112
FT                   /note="PRPP-binding"
FT                   /evidence="ECO:0000250"
FT   BINDING         40..41
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         104..112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   STRAND          2..7
FT                   /evidence="ECO:0007829|PDB:2IGB"
FT   HELIX           9..27
FT                   /evidence="ECO:0007829|PDB:2IGB"
FT   STRAND          33..38
FT                   /evidence="ECO:0007829|PDB:2IGB"
FT   HELIX           39..57
FT                   /evidence="ECO:0007829|PDB:2IGB"
FT   STRAND          63..72
FT                   /evidence="ECO:0007829|PDB:2IGB"
FT   STRAND          82..90
FT                   /evidence="ECO:0007829|PDB:2IGB"
FT   STRAND          98..110
FT                   /evidence="ECO:0007829|PDB:2IGB"
FT   HELIX           111..121
FT                   /evidence="ECO:0007829|PDB:2IGB"
FT   STRAND          127..136
FT                   /evidence="ECO:0007829|PDB:2IGB"
FT   STRAND          141..143
FT                   /evidence="ECO:0007829|PDB:2IGB"
FT   STRAND          147..152
FT                   /evidence="ECO:0007829|PDB:2IGB"
FT   STRAND          159..164
FT                   /evidence="ECO:0007829|PDB:2IGB"
FT   HELIX           166..169
FT                   /evidence="ECO:0007829|PDB:2IGB"
FT   STRAND          173..178
FT                   /evidence="ECO:0007829|PDB:2IGB"
SQ   SEQUENCE   179 AA;  19938 MW;  DF889A00B239CFB5 CRC64;
     MQKAVVMDEQ AIRRALTRIA HEIIERNKGI DGCVLVGIKT RGIYLARRLA ERIEQIEGAS
     VPVGELDITL YRDDLTVKTD DHEPLVKGTN VPFPVTERNV ILVDDVLFTG RTVRAAMDAV
     MDLGRPARIQ LAVLVDRGHR ELPIRADFVG KNVPTSRSEL IVVELSEVDG IDQVSIHEK