ID   PURR_YERE8              Reviewed;         341 AA.
AC   A1JP52;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=HTH-type transcriptional repressor PurR {ECO:0000255|HAMAP-Rule:MF_01277};
DE   AltName: Full=Pur regulon repressor {ECO:0000255|HAMAP-Rule:MF_01277};
DE   AltName: Full=Purine nucleotide synthesis repressor {ECO:0000255|HAMAP-Rule:MF_01277};
GN   Name=purR {ECO:0000255|HAMAP-Rule:MF_01277}; OrderedLocusNames=YE2158;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
CC   -!- FUNCTION: Is the main repressor of the genes involved in the de novo
CC       synthesis of purine nucleotides, regulating purB, purC, purEK, purF,
CC       purHD, purL, purMN and guaBA expression. PurR is allosterically
CC       activated to bind its cognate DNA by binding the purine corepressors,
CC       hypoxanthine or guanine, thereby effecting transcription repression.
CC       {ECO:0000255|HAMAP-Rule:MF_01277}.
CC   -!- PATHWAY: Purine metabolism; purine nucleotide biosynthesis
CC       [regulation].
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01277}.
CC   -!- DOMAIN: Consists of two structural and functional domains: an N-
CC       terminal DNA-binding domain, approximately the first 60 residues, and a
CC       larger C-terminal domain, approximately 280 residues, which imparts the
CC       function of corepressor binding and oligomerization.
CC       {ECO:0000255|HAMAP-Rule:MF_01277}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM286415; CAL12228.1; -; Genomic_DNA.
DR   RefSeq; WP_005165644.1; NC_008800.1.
DR   RefSeq; YP_001006398.1; NC_008800.1.
DR   AlphaFoldDB; A1JP52; -.
DR   SMR; A1JP52; -.
DR   STRING; 393305.YE2158; -.
DR   EnsemblBacteria; CAL12228; CAL12228; YE2158.
DR   GeneID; 67418200; -.
DR   KEGG; yen:YE2158; -.
DR   PATRIC; fig|393305.7.peg.2323; -.
DR   eggNOG; COG1609; Bacteria.
DR   HOGENOM; CLU_037628_6_2_6; -.
DR   OMA; ARWVGPP; -.
DR   UniPathway; UPA00488; -.
DR   Proteomes; UP000000642; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01392; HTH_LacI; 1.
DR   Gene3D; 1.10.260.40; -; 1.
DR   HAMAP; MF_01277; HTH_type_PurR; 1.
DR   InterPro; IPR000843; HTH_LacI.
DR   InterPro; IPR046335; LacI/GalR-like_sensor.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   InterPro; IPR023588; Tscrpt_reg_HTH_PurR.
DR   Pfam; PF00356; LacI; 1.
DR   Pfam; PF13377; Peripla_BP_3; 1.
DR   PRINTS; PR00036; HTHLACI.
DR   SMART; SM00354; HTH_LACI; 1.
DR   SUPFAM; SSF47413; SSF47413; 1.
DR   SUPFAM; SSF53822; SSF53822; 1.
DR   PROSITE; PS00356; HTH_LACI_1; 1.
DR   PROSITE; PS50932; HTH_LACI_2; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Purine biosynthesis; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..341
FT                   /note="HTH-type transcriptional repressor PurR"
FT                   /id="PRO_1000085880"
FT   DOMAIN          2..56
FT                   /note="HTH lacI-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01277"
FT   DNA_BIND        4..23
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01277"
FT   DNA_BIND        48..56
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01277"
FT   BINDING         73
FT                   /ligand="hypoxanthine"
FT                   /ligand_id="ChEBI:CHEBI:17368"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01277"
FT   BINDING         190
FT                   /ligand="hypoxanthine"
FT                   /ligand_id="ChEBI:CHEBI:17368"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01277"
FT   BINDING         192
FT                   /ligand="hypoxanthine"
FT                   /ligand_id="ChEBI:CHEBI:17368"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01277"
FT   BINDING         221
FT                   /ligand="hypoxanthine"
FT                   /ligand_id="ChEBI:CHEBI:17368"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01277"
FT   BINDING         275
FT                   /ligand="hypoxanthine"
FT                   /ligand_id="ChEBI:CHEBI:17368"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01277"
SQ   SEQUENCE   341 AA;  37873 MW;  4D7556B58D0FA6CD CRC64;
     MATIKDVAKH AGVSTTTVSH VINKTRFVAE NTKAAVWAAI KELHYSPSAV ARSLKVNHTK
     SIGLLATSSE APYFAEVIEA VENSCYSKGY TLILCNSHNN LDKQKAYLAM LAQKRVDGLL
     VMCSEYPEQL LGMLEDYRNI PMVVMDWGTA RGDFTDSIID NAFEGGYLAG RYLIERGHRD
     IGAIPGQLSR NTGGGRHQGF LKALEEANIT LREEWVVQGD FEPESGYKAM HQILTQKHRP
     TAVFCGGDIM AMGAICAADE LGLRVPQDIS VIGYDNVRNA RYFSPALTTI HQPKERLGET
     AFAMLLDRIV SKREDPQTIE VHPKLVERRS VADGPFRDYR R