ID   TFDR_CUPPJ              Reviewed;         295 AA.
AC   Q46M57; P10086; P42429;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=HTH-type transcriptional regulator TdfR;
GN   Name=tfdR; OrderedLocusNames=Reut_D6475;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OG   Plasmid pJP4, and Plasmid pPJ4.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DNA-BINDING.
RC   PLASMID=pJP4;
RX   PubMed=8157603; DOI=10.1128/jb.176.8.2348-2353.1994;
RA   Matrubutham U., Harker A.R.;
RT   "Analysis of duplicated gene sequences associated with tfdR and tfdS in
RT   Alcaligenes eutrophus JMP134.";
RL   J. Bacteriol. 176:2348-2353(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pJP4;
RX   PubMed=15186344; DOI=10.1111/j.1462-2920.2004.00596.x;
RA   Trefault N., De la Iglesia R., Molina A.M., Manzano M., Ledger T.,
RA   Perez-Pantoja D., Sanchez M.A., Stuardo M., Gonzalez B.;
RT   "Genetic organization of the catabolic plasmid pJP4 from Ralstonia eutropha
RT   JMP134 (pJP4) reveals mechanisms of adaptation to chloroaromatic pollutants
RT   and evolution of specialized chloroaromatic degradation pathways.";
RL   Environ. Microbiol. 6:655-668(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197; PLASMID=pPJ4;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(2010).
RN   [4]
RP   IDENTIFICATION OF PROTEIN, AND POSSIBLE DNA-BINDING REGION.
RX   PubMed=3413113; DOI=10.1073/pnas.85.18.6602;
RA   Henikoff S., Haughn G.W., Calvo J.M., Wallace J.C.;
RT   "A large family of bacterial activator proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:6602-6606(1988).
CC   -!- FUNCTION: Involved in the regulation of 3-chlorocatechol degradation.
CC       Transcriptional regulator of tfdB expression. Acts as a repressor in
CC       the absence of its effector (either 2-cis-chlorodiene lactone or
CC       chloromaleylacetate) but acts as an activator when its effector is
CC       present.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family.
CC       {ECO:0000305}.
CC   -!- CAUTION: The products of the genes tfdR and tfdS were originally
CC       thought to be identical but in fact they differ by one residue (amino
CC       acid 264 which is Asp in tfdR and Ala in tfdS). {ECO:0000305}.
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; M98445; AAA65063.1; -; Genomic_DNA.
DR   EMBL; AY365053; AAR31048.1; -; Genomic_DNA.
DR   EMBL; CP000093; AAZ65773.1; -; Genomic_DNA.
DR   RefSeq; WP_011178395.1; NZ_AY365053.1.
DR   AlphaFoldDB; Q46M57; -.
DR   SMR; Q46M57; -.
DR   EnsemblBacteria; AAZ65773; AAZ65773; Reut_D6475.
DR   KEGG; reu:Reut_D6475; -.
DR   HOGENOM; CLU_039613_6_4_4; -.
DR   OMA; EQVREND; -.
DR   OrthoDB; 1439189at2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR005119; LysR_subst-bd.
DR   InterPro; IPR000847; Tscrpt_reg_HTH_LysR.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00126; HTH_1; 1.
DR   Pfam; PF03466; LysR_substrate; 1.
DR   PRINTS; PR00039; HTHLYSR.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS50931; HTH_LYSR; 1.
PE   1: Evidence at protein level;
KW   Activator; Aromatic hydrocarbons catabolism; Cytoplasm; DNA-binding;
KW   Plasmid; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..295
FT                   /note="HTH-type transcriptional regulator TdfR"
FT                   /id="PRO_0000105760"
FT   DOMAIN          1..58
FT                   /note="HTH lysR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT   DNA_BIND        18..37
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
SQ   SEQUENCE   295 AA;  32070 MW;  C6C477BE8127A41A CRC64;
     MEFRQLRYFV AAAEEGNVGA AARRLHISQP PVTRQIHALE QHLGVLLFER SARGVQLTPA
     GAAFLEDARR MLELGRTSVD RSRAASRGEI GQLDIGYLGT AIYQTVPALL HAFTQAVPGA
     TLSLALMPKV RQIEALRAGT IHLGVGRFYP QEPGITVEHL HYERLYIAAG SSIARQLRQD
     PTLLRLKSES LVLFPKEGRP SFADEVIALM RRAGVEPRVT AIVEDVNAAL GLVAAGAGVT
     LVPASVAAIR RPFVRTMEMA DASDKVPVSL TYLTDSRVPV LRAFLDVARR GKGQK