ID   PURR_KLEP7              Reviewed;         341 AA.
AC   A6TA06;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
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};
GN   OrderedLocusNames=KPN78578_19660; ORFNames=KPN_01996;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000647; ABR77427.1; -; Genomic_DNA.
DR   RefSeq; WP_002907778.1; NC_009648.1.
DR   AlphaFoldDB; A6TA06; -.
DR   SMR; A6TA06; -.
DR   STRING; 272620.KPN_01996; -.
DR   jPOST; A6TA06; -.
DR   EnsemblBacteria; ABR77427; ABR77427; KPN_01996.
DR   KEGG; kpn:KPN_01996; -.
DR   HOGENOM; CLU_037628_6_2_6; -.
DR   OMA; ARWVGPP; -.
DR   UniPathway; UPA00488; -.
DR   Proteomes; UP000000265; 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_1000085874"
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;  38061 MW;  BE2767D505A57FF8 CRC64;
     MATIKDVAKR ANVSTTTVSH VINKTRFVAE ETRNAVWAAI KELHYSPSAV ARSLKVNHTK
     SIGLLATSSE AAYFAEIIES VEKSCFQKGY TLILGNAWND LEKQRAYLSM MAQKRVDGLL
     VMCSEYPDSV LSMLEEYRHI PMVVMDWGEA KADFTDAVID NAFQGGYIAG RYLIERGHRE
     IGVIPGPLER NTGAGRLAGF MQAMKEAHIS VPENWIVQGD FEPESGYRAM QQILNQQHRP
     TAVFCGGDIM AMGAICAADE MGLRVPQDIS LIGYDNVRNA RYFSPALTTI HQPKDSLGEA
     AFNMLLDRIV NKREESQSIE VHPRLVERRS VADGPFVDYR R