TFDS_CUPPJ
ID TFDS_CUPPJ Reviewed; 295 AA.
AC Q46M54; P10086; P42429; P95668;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=HTH-type transcriptional regulator TfdS;
GN Name=tfdS; Synonyms=tfdO; OrderedLocusNames=Reut_D6478;
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].
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], AND EXPRESSION IN PSEUDOMONAS CEPACIA
RP 383.
RC PLASMID=pJP4;
RX PubMed=7565094; DOI=10.1111/j.1365-2958.1995.tb02304.x;
RA You I.S., Ghosal D.;
RT "Genetic and molecular analysis of a regulatory region of the herbicide
RT 2,4-dichlorophenoxyacetate catabolic plasmid pJP4.";
RL Mol. Microbiol. 16:321-331(1995).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-180.
RC PLASMID=pJP4;
RX PubMed=3036764; DOI=10.1128/jb.169.7.2950-2955.1987;
RA Streber W.R., Timmis K.N., Zenk M.H.;
RT "Analysis, cloning, and high-level expression of 2,4-dichlorophenoxyacetate
RT monooxygenase gene tfdA of Alcaligenes eutrophus JMP134.";
RL J. Bacteriol. 169:2950-2955(1987).
RN [6]
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}.
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DR EMBL; S80112; AAB47014.2; -; Genomic_DNA.
DR EMBL; AY365053; AAR31051.1; -; Genomic_DNA.
DR EMBL; CP000093; AAZ65776.1; -; Genomic_DNA.
DR EMBL; M16730; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; WP_011178398.1; NZ_AY365053.1.
DR AlphaFoldDB; Q46M54; -.
DR SMR; Q46M54; -.
DR EnsemblBacteria; AAZ65776; AAZ65776; Reut_D6478.
DR GeneID; 55536830; -.
DR KEGG; reu:Reut_D6478; -.
DR HOGENOM; CLU_039613_6_4_4; -.
DR OMA; ERSHRGI; -.
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 TfdS"
FT /id="PRO_0000105761"
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"
FT CONFLICT 264
FT /note="A -> D (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 295 AA; 32026 MW; B1B407BE8127A41F 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 DASAKVPVSL TYLTDSRVPV LRAFLDVARR GKGQK
