ID DTXR_CORDI Reviewed; 226 AA. AC P0DJL7; P33120; Q5XQ41; Q5XQ42; Q5XQ43; DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2012, sequence version 1. DT 09-DEC-2015, entry version 29. DE RecName: Full=Diphtheria toxin repressor; DE AltName: Full=Iron-dependent diphtheria tox regulatory element; DE AltName: Full=Tox regulatory factor; GN Name=dtxR; OrderedLocusNames=DIP1414; OS Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype OS gravis). OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=257309; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=C7(-); RX PubMed=2116013; DOI=10.1073/pnas.87.15.5968; RA Boyd J.M., Oza M.N., Murphy J.R.; RT "Molecular cloning and DNA sequence analysis of a diphtheria tox iron- RT dependent regulatory element (dtxR) from Corynebacterium RT diphtheriae."; RL Proc. Natl. Acad. Sci. U.S.A. 87:5968-5972(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=1030(-), and C7hm723(-); RX PubMed=1735717; RA Boyd J.M., Hall K.C., Murphy J.R.; RT "DNA sequences and characterization of dtxR alleles from RT Corynebacterium diphtheriae PW8(-), 1030(-), and C7hm723(-)."; RL J. Bacteriol. 174:1268-1272(1992). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND STUDY OF FUNCTIONALITY. RC STRAIN=CD95/211-, CD95/305-, and CD95/407-; RX PubMed=15634975; DOI=10.1128/JCM.43.1.223-228.2005; RA De Zoysa A.S., Efstratiou A., Hawkey P.M.; RT "Molecular characterization of diphtheria toxin repressor (dtxR) genes RT present in nontoxigenic Corynebacterium diphtheriae strains isolated RT in the United Kingdom."; RL J. Clin. Microbiol. 43:223-228(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis; RX PubMed=14602910; DOI=10.1093/nar/gkg874; RA Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G., RA Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D., RA De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., RA Hamlin N., Holroyd S., Jagels K., Moule S., Quail M.A., RA Rabbinowitsch E., Rutherford K.M., Thomson N.R., Unwin L., RA Whitehead S., Barrell B.G., Parkhill J.; RT "The complete genome sequence and analysis of Corynebacterium RT diphtheriae NCTC13129."; RL Nucleic Acids Res. 31:6516-6523(2003). RN [5] RP CHARACTERIZATION. RX PubMed=1502169; DOI=10.1073/pnas.89.16.7576; RA Schmitt M.P., Twiddy E.M., Holmes R.K.; RT "Purification and characterization of the diphtheria toxin RT repressor."; RL Proc. Natl. Acad. Sci. U.S.A. 89:7576-7580(1992). RN [6] RP METAL-BINDING. RX PubMed=1400485; RA Tao X., Murphy J.R.; RT "Binding of the metalloregulatory protein DtxR to the diphtheria tox RT operator requires a divalent heavy metal ion and protects the RT palindromic sequence from DNase I digestion."; RL J. Biol. Chem. 267:21761-21764(1992). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=8823163; DOI=10.1021/bi960861d; RA Qiu X., Pohl E., Holmes R.K., Hol W.G.J.; RT "High-resolution structure of the diphtheria toxin repressor complexed RT with cobalt and manganese reveals an SH3-like third domain and RT suggests a possible role of phosphate as co-corepressor."; RL Biochemistry 35:12292-12302(1996). RN [8] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). RX PubMed=7568230; DOI=10.1073/pnas.92.21.9843; RA Schiering N., Tao X., Zeng H., Murphy J.R., Petsko G.A., Ringe D.; RT "Structures of the apo- and the metal ion-activated forms of the RT diphtheria tox repressor from Corynebacterium diphtheriae."; RL Proc. Natl. Acad. Sci. U.S.A. 92:9843-9850(1995). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RX PubMed=9697776; DOI=10.1038/28893; RA White A., Ding X., Vanderspek J.C., Murphy J.R., Ringe D.; RT "Structure of the metal-ion-activated diphtheria toxin repressor/tox RT operator complex."; RL Nature 394:502-506(1998). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RX PubMed=10085021; RA Goranson-Siekierke J., Pohl E., Hol W.G.J., Holmes R.K.; RT "Anion-coordinating residues at binding site 1 are essential for the RT biological activity of the diphtheria toxin repressor."; RL Infect. Immun. 67:1806-1811(1999). RN [11] RP STRUCTURE BY NMR OF 130-226. RX PubMed=10339551; DOI=10.1073/pnas.96.11.6119; RA Wang G., Wylie G.P., Twigg P.D., Caspar D.L.D., Murphy J.R., RA Logan T.M.; RT "Solution structure and peptide binding studies of the C-terminal src RT homology 3-like domain of the diphtheria toxin repressor protein."; RL Proc. Natl. Acad. Sci. U.S.A. 96:6119-6124(1999). CC -!- FUNCTION: Iron-binding repressor of the dipheteria toxin gene CC expression. May serve as a global regulator of gene expression. CC Represses ripA under iron excess. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- MISCELLANEOUS: The N-terminal region may be involved in iron CC binding and may associate with the tox operator. Binding of dtxR CC to tox operator requires a divalent metal ion such as cobalt, CC ferric, manganese, and nickel ions whereas zinc ions show weak CC activation. CC -!- MISCELLANEOUS: The dtxR gene was functional in the non-toxygenic CC strains CD95/211-, CD95/305- and CD95/407- isolated in the United CC Kingdom. These findings demonstrate that, if lysogenised by a CC bacteriophage, non-toxygenic strains could produce toxin and CC therefore represent a potential reservoir for toxygenic CC C.diphtheriae. CC -!- SIMILARITY: Contains 1 HTH dtxR-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00296}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M34239; AAA23296.1; -; Genomic_DNA. DR EMBL; M80336; AAA23302.1; -; Genomic_DNA. DR EMBL; M80337; AAA23301.1; -; Genomic_DNA. DR EMBL; AY741368; AAU93781.1; -; Genomic_DNA. DR EMBL; AY741369; AAU93782.1; -; Genomic_DNA. DR EMBL; AY741370; AAU93783.1; -; Genomic_DNA. DR EMBL; BX248358; CAE49945.1; -; Genomic_DNA. DR PIR; A35968; A35968. DR RefSeq; WP_010935052.1; NC_002935.2. DR PDB; 1BI0; X-ray; 2.30 A; A=1-226. DR PDB; 1BI1; X-ray; 2.20 A; A=1-226. DR PDB; 1BI2; X-ray; 2.30 A; A/B=1-226. DR PDB; 1BI3; X-ray; 2.40 A; A/B=1-226. DR PDB; 1BYM; NMR; -; A=130-226. DR PDB; 1C0W; X-ray; 3.20 A; A/B/C/D=2-226. DR PDB; 1DDN; X-ray; 3.00 A; A/B/C/D=1-226. DR PDB; 1DPR; X-ray; 3.00 A; A/B=1-226. DR PDB; 1F5T; X-ray; 3.00 A; A/B/C/D=1-121. DR PDB; 1FWZ; X-ray; 2.30 A; A=1-226. DR PDB; 1G3S; X-ray; 2.40 A; A=1-226. DR PDB; 1G3T; X-ray; 2.35 A; A/B=1-226. DR PDB; 1G3W; X-ray; 2.40 A; A=1-226. DR PDB; 1G3Y; X-ray; 2.80 A; A=1-226. DR PDB; 1P92; X-ray; 2.10 A; A=1-226. DR PDB; 1QVP; NMR; -; A=148-226. DR PDB; 1QW1; NMR; -; A=110-226. DR PDB; 1XCV; X-ray; 2.10 A; A=1-139. DR PDB; 2DTR; X-ray; 1.90 A; A=1-226. DR PDB; 2QQ9; X-ray; 1.71 A; A=1-226. DR PDB; 2QQA; X-ray; 2.10 A; A=1-226. DR PDB; 2QQB; X-ray; 1.92 A; A=1-226. DR PDB; 2TDX; X-ray; 2.40 A; A=1-226. DR PDB; 3GLX; X-ray; 1.85 A; A=1-226. DR PDBsum; 1BI0; -. DR PDBsum; 1BI1; -. DR PDBsum; 1BI2; -. DR PDBsum; 1BI3; -. DR PDBsum; 1BYM; -. DR PDBsum; 1C0W; -. DR PDBsum; 1DDN; -. DR PDBsum; 1DPR; -. DR PDBsum; 1F5T; -. DR PDBsum; 1FWZ; -. DR PDBsum; 1G3S; -. DR PDBsum; 1G3T; -. DR PDBsum; 1G3W; -. DR PDBsum; 1G3Y; -. DR PDBsum; 1P92; -. DR PDBsum; 1QVP; -. DR PDBsum; 1QW1; -. DR PDBsum; 1XCV; -. DR PDBsum; 2DTR; -. DR PDBsum; 2QQ9; -. DR PDBsum; 2QQA; -. DR PDBsum; 2QQB; -. DR PDBsum; 2TDX; -. DR PDBsum; 3GLX; -. DR DisProt; DP00374; -. DR ProteinModelPortal; P0DJL7; -. DR SMR; P0DJL7; 2-226. DR EnsemblBacteria; CAE49945; CAE49945; DIP1414. DR GeneID; 2649688; -. DR KEGG; cdi:DIP1414; -. DR KO; K03709; -. DR OMA; TEATIVQ; -. DR Proteomes; UP000002198; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 1.10.60.10; -; 1. DR InterPro; IPR007167; Fe-transptr_FeoA. DR InterPro; IPR001367; Fe_dep_repressor. DR InterPro; IPR022687; HTH_DTXR. DR InterPro; IPR022689; Iron_dep_repressor. DR InterPro; IPR008988; Transcriptional_repressor_C. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF02742; Fe_dep_repr_C; 1. DR Pfam; PF01325; Fe_dep_repress; 1. DR SMART; SM00899; FeoA; 1. DR SMART; SM00529; HTH_DTXR; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF47979; SSF47979; 1. DR SUPFAM; SSF50037; SSF50037; 1. DR PROSITE; PS50944; HTH_DTXR; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; DNA-binding; Iron; KW Reference proteome; Repressor; Transcription; KW Transcription regulation. FT CHAIN 1 226 Diphtheria toxin repressor. FT /FTId=PRO_0000201106. FT DOMAIN 4 65 HTH dtxR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00296}. FT VARIANT 47 47 R -> H (in iron-insensitive tox FT constitutive mutant C7hm723). FT VARIANT 141 141 G -> R (in strain: CD95/211-). FT VARIANT 147 147 V -> A (in strain: C7(-), C7hm723(-), FT 1030(-), CD95/305-, CD95/211- and CD95/ FT 407-). FT VARIANT 165 165 I -> V (in strain: 1030(-)). FT VARIANT 174 174 V -> A (in strain: 1030(-)). FT VARIANT 191 191 S -> T (in strain: 1030(-)). FT VARIANT 199 199 D -> V (in strain: CD95/407-). FT VARIANT 201 201 H -> R (in strain: CD95/305-). FT VARIANT 205 205 S -> R (in strain: 1030(-)). FT VARIANT 214 214 I -> L (in strain: C7(-), C7hm723(-), FT CD95/305-, CD95/211- and CD95/407-). FT VARIANT 214 214 I -> Y (in strain: 1030(-)). FT VARIANT 218 218 A -> T (in strain: 1030(-)). FT VARIANT 221 221 I -> M (in strain: CD95/211-). FT VARIANT 221 221 I -> T (in strain: CD95/407-). FT HELIX 4 21 {ECO:0000244|PDB:2QQ9}. FT HELIX 27 34 {ECO:0000244|PDB:2QQ9}. FT HELIX 38 50 {ECO:0000244|PDB:2QQ9}. FT STRAND 53 56 {ECO:0000244|PDB:2QQ9}. FT STRAND 60 64 {ECO:0000244|PDB:2QQ9}. FT HELIX 66 88 {ECO:0000244|PDB:2QQ9}. FT HELIX 94 104 {ECO:0000244|PDB:2QQ9}. FT TURN 105 107 {ECO:0000244|PDB:2QQ9}. FT HELIX 110 119 {ECO:0000244|PDB:2QQ9}. FT STRAND 127 130 {ECO:0000244|PDB:1DPR}. FT HELIX 135 138 {ECO:0000244|PDB:2QQ9}. FT STRAND 145 148 {ECO:0000244|PDB:1QW1}. FT STRAND 149 151 {ECO:0000244|PDB:2QQA}. FT HELIX 152 155 {ECO:0000244|PDB:2QQ9}. FT STRAND 161 167 {ECO:0000244|PDB:2QQ9}. FT HELIX 170 172 {ECO:0000244|PDB:2QQ9}. FT HELIX 177 184 {ECO:0000244|PDB:2QQ9}. FT STRAND 188 195 {ECO:0000244|PDB:2QQ9}. FT STRAND 197 199 {ECO:0000244|PDB:1P92}. FT STRAND 203 208 {ECO:0000244|PDB:2QQ9}. FT STRAND 210 212 {ECO:0000244|PDB:2QQ9}. FT HELIX 215 220 {ECO:0000244|PDB:2QQ9}. FT STRAND 222 224 {ECO:0000244|PDB:2QQ9}. SQ SEQUENCE 226 AA; 25344 MW; A14F89FDB8719D5C CRC64; MKDLVDTTEM YLRTIYELEE EGVTPLRARI AERLEQSGPT VSQTVARMER DGLVVVASDR SLQMTPTGRT LATAVMRKHR LAERLLTDII GLDINKVHDE ACRWEHVMSD EVERRLVKVL KDVSRSPFGN PIPGLDELGV GNSDAAVPGT RVIDAATSMP RKVRIVQINE IFQVETDQFT QLLDADIRVG SEVEIVDRDG HITLSHNGKD VELIDDLAHT IRIEEL //