ID   PURR_VIBVY              Reviewed;         334 AA.
AC   Q7MJ57;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 119.
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=VV2305;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
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}.
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DR   EMBL; BA000037; BAC95069.1; -; Genomic_DNA.
DR   RefSeq; WP_011080017.1; NC_005139.1.
DR   AlphaFoldDB; Q7MJ57; -.
DR   SMR; Q7MJ57; -.
DR   STRING; 672.VV93_v1c20170; -.
DR   EnsemblBacteria; BAC95069; BAC95069; BAC95069.
DR   KEGG; vvy:VV2305; -.
DR   eggNOG; COG1609; Bacteria.
DR   HOGENOM; CLU_037628_6_2_6; -.
DR   OMA; ARWVGPP; -.
DR   OrthoDB; 1796334at2; -.
DR   UniPathway; UPA00488; -.
DR   Proteomes; UP000002675; Chromosome I.
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; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..334
FT                   /note="HTH-type transcriptional repressor PurR"
FT                   /id="PRO_0000279676"
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         189
FT                   /ligand="hypoxanthine"
FT                   /ligand_id="ChEBI:CHEBI:17368"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01277"
FT   BINDING         220
FT                   /ligand="hypoxanthine"
FT                   /ligand_id="ChEBI:CHEBI:17368"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01277"
FT   BINDING         274
FT                   /ligand="hypoxanthine"
FT                   /ligand_id="ChEBI:CHEBI:17368"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01277"
SQ   SEQUENCE   334 AA;  37756 MW;  D4F3502AD4B34CD6 CRC64;
     MATIKDVARL AGVSTTTVSH VINKTRFVAE ATQEKVMKAV DELNYAPSAV ARSLKCNTTR
     TIGMLVTQST NLFFSEVIDG VESYCYRQGY TLILCNTGGI YEKQRDYIRM LAEKRVDGIL
     VMCSDLTEEL REMLDKHADI PKVIMDWGPI SSQADKIIDN SEEGGYLATK YLIDNGHTKI
     ACLSGHFEKA ACQERIQGFK RAMKEANITL NNEWILEGNF ECDTAVMAAD KIASWQDRPT
     AVFCFNDTMA LGLMSRLQQL GLRIPEDISV IGYDNIELAE YFSPPLTTIH QPKRRVGKNA
     FEILLERIKD KEHDKRVFEM HPELVVRDTV KKIN