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Entry: PURR_SALTY
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ID   PURR_SALTY              Reviewed;         341 AA.
AC   O68446;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 148.
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=STM1430;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RA   Katzif S.D., Lu C.D., Abdelal A.T.;
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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; AF040636; AAC05741.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL20352.1; -; Genomic_DNA.
DR   RefSeq; NP_460393.1; NC_003197.2.
DR   RefSeq; WP_000190993.1; NC_003197.2.
DR   AlphaFoldDB; O68446; -.
DR   SMR; O68446; -.
DR   STRING; 99287.STM1430; -.
DR   PaxDb; 99287-STM1430; -.
DR   GeneID; 1252948; -.
DR   KEGG; stm:STM1430; -.
DR   PATRIC; fig|99287.12.peg.1512; -.
DR   HOGENOM; CLU_037628_6_2_6; -.
DR   OMA; MDWGPES; -.
DR   PhylomeDB; O68446; -.
DR   BioCyc; SENT99287:STM1430-MONOMER; -.
DR   UniPathway; UPA00488; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR   CDD; cd01392; HTH_LacI; 1.
DR   CDD; cd06275; PBP1_PurR; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 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   PANTHER; PTHR30146:SF152; HTH-TYPE TRANSCRIPTIONAL REGULATOR EBGR-RELATED; 1.
DR   PANTHER; PTHR30146; LACI-RELATED TRANSCRIPTIONAL REPRESSOR; 1.
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; lambda repressor-like DNA-binding domains; 1.
DR   SUPFAM; SSF53822; Periplasmic binding protein-like I; 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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..341
FT                   /note="HTH-type transcriptional repressor PurR"
FT                   /id="PRO_0000107981"
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;  38048 MW;  23C0C9B7E8B222DC CRC64;
     MATIKDVAKR ANVSTTTVSH VINKTRFVAE ETRNAVWAAI KELHYSPSAV ARSLKVNHTK
     SIGLLATSSE AAYFAEIIEA VEKNCFQKGY TLILGNAWNN LEKQRAYLSM MAQKRVDGLL
     VMCSEYPEPL LSMLEEYRHI PMVVMDWGEA KADFTDTVID NAFAGGYMAG RYLVERGHRD
     IGVIPGPLER NTGAGRLAGF MKAMEEALIN VPDNWIVQGD FEPESGYHAM QQILSQSHRP
     TAVFCGGDIM AMGALCAADE MGLRVPQDVS VIGYDNVRNA RYFTPALTTI HQPKDSLGET
     AFNMLLDRIV NKREESQSIE VHPRLVERRS VADGPFRDYR R
//
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