PURR_SALTI
ID PURR_SALTI Reviewed; 341 AA.
AC Q8Z6P1; Q7CA30;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, 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};
GN OrderedLocusNames=STY1692, t1298;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(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; AL513382; CAD01937.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO68948.1; -; Genomic_DNA.
DR RefSeq; NP_456100.1; NC_003198.1.
DR RefSeq; WP_000190992.1; NZ_WSUR01000011.1.
DR AlphaFoldDB; Q8Z6P1; -.
DR SMR; Q8Z6P1; -.
DR STRING; 220341.16502779; -.
DR EnsemblBacteria; AAO68948; AAO68948; t1298.
DR KEGG; stt:t1298; -.
DR KEGG; sty:STY1692; -.
DR PATRIC; fig|220341.7.peg.1702; -.
DR eggNOG; COG1609; Bacteria.
DR HOGENOM; CLU_037628_6_2_6; -.
DR OMA; ARWVGPP; -.
DR UniPathway; UPA00488; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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_0000279667"
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; 38032 MW; 23C0C9A8F7B23DC3 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 RFFTPALTTI HQPKDSLGET
AFNMLLDRIV NKREESQSIE VHPRLVERRS VADGPFRDYR R
