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PURR_PHOLL
ID   PURR_PHOLL              Reviewed;         341 AA.
AC   Q7N3V8;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 124.
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=plu2605;
OS   Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS   TT01).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=243265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15139 / CIP 105565 / TT01;
RX   PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA   Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA   Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(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; BX571867; CAE14979.1; -; Genomic_DNA.
DR   RefSeq; WP_011146827.1; NC_005126.1.
DR   AlphaFoldDB; Q7N3V8; -.
DR   SMR; Q7N3V8; -.
DR   STRING; 243265.plu2605; -.
DR   EnsemblBacteria; CAE14979; CAE14979; plu2605.
DR   GeneID; 24166056; -.
DR   KEGG; plu:plu2605; -.
DR   eggNOG; COG1609; Bacteria.
DR   HOGENOM; CLU_037628_6_2_6; -.
DR   OMA; ARWVGPP; -.
DR   OrthoDB; 1796334at2; -.
DR   BioCyc; PLUM243265:PLU_RS12895-MON; -.
DR   UniPathway; UPA00488; -.
DR   Proteomes; UP000002514; 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; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..341
FT                   /note="HTH-type transcriptional repressor PurR"
FT                   /id="PRO_0000279664"
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;  37913 MW;  0324A4167BB17D22 CRC64;
     MATIKDVAKH AGVSTTTVSH VINKTRFVAE DTKAAVWAAI KALNYSPSAV ARSLKVNHTK
     SIGLLATSSE APYFAEIIES VENSCYSKGY TLILCNSHNN IDKQKAYLAM LAQKRVDGLL
     IMCSEYPEQL LGMLEDYRNI PMVVMDWGQA RSDFTDTIID NAFHGGYLAG RYLIERGHRD
     IGAIPGPLAR NTGGGRHQGF LKALKEANIP IKEEWVIQGD FEPESGYKAM HQILNQKQRP
     TAVFCGGDVM AMGAICAADE LGLRVPQDIS VIGYDNIRNA RYFSPALTTI HQPKERLGQM
     AFSMLLDRII NKREDAQTIE VHPRLVERRS VVDGPFVDYR R
 
 
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