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TFDT_CUPPJ
ID   TFDT_CUPPJ              Reviewed;         228 AA.
AC   P42427; Q46M65;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 135.
DE   RecName: Full=HTH-type transcriptional regulator TfdT;
GN   Name=tfdT; OrderedLocusNames=Reut_D6467;
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=8955303; DOI=10.1128/jb.178.23.6824-6832.1996;
RA   Leveau J.H., van der Meer J.R.;
RT   "The tfdR gene product can successfully take over the role of the insertion
RT   element-inactivated TfdT protein as a transcriptional activator of the
RT   tfdCDEF gene cluster, which encodes chlorocatechol degradation in Ralstonia
RT   eutropha JMP134(pJP4).";
RL   J. Bacteriol. 178:6824-6832(1996).
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-47.
RC   PLASMID=pJP4;
RX   PubMed=2185214; DOI=10.1128/jb.172.5.2351-2359.1990;
RA   Perkins E.J., Gordon M.P., Caceres O., Lurquin P.F.;
RT   "Organization and sequence analysis of the 2,4-dichlorophenol hydroxylase
RT   and dichlorocatechol oxidative operons of plasmid pJP4.";
RL   J. Bacteriol. 172:2351-2359(1990).
CC   -!- FUNCTION: Does not seem to be involved in the regulation of 3-
CC       chlorocatechol degradation. Does not activate the expression of its
CC       presumed target operon, tfdCDEF.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family.
CC       {ECO:0000305}.
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DR   EMBL; U16782; AAC44724.1; -; Genomic_DNA.
DR   EMBL; AY365053; AAR31040.1; -; Genomic_DNA.
DR   EMBL; CP000093; AAZ65765.1; -; Genomic_DNA.
DR   EMBL; M35097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; S03396; S03396.
DR   RefSeq; WP_011178387.1; NZ_AY365053.1.
DR   AlphaFoldDB; P42427; -.
DR   SMR; P42427; -.
DR   STRING; 264198.Reut_C6411; -.
DR   EnsemblBacteria; AAZ65765; AAZ65765; Reut_D6467.
DR   KEGG; reu:Reut_D6467; -.
DR   HOGENOM; CLU_039613_6_4_4; -.
DR   OMA; WNIGTET; -.
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   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; Cytoplasm; DNA-binding; Plasmid;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..228
FT                   /note="HTH-type transcriptional regulator TfdT"
FT                   /id="PRO_0000105762"
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   228 AA;  24965 MW;  55842D70BCE7313E CRC64;
     MEIRQLKYFV AVAEAGGFGT AAQRMHISQP PLTRQIQALE RDIGAKLFER TARGVELTAA
     GKVFLDDARQ LLALVQRSSR RSQAAARGES GELKLVYFGT PVFETVPAFV RTFLATYPDA
     TVAVSHMTKE AQLESLLSGV VDIGFGRFYP VTEGVSSWNI GTETLHVAAA DPWDTRVSRA
     RAVVDLLDVP LILYPRGDRP SFADKVVSIF RDRFKKSPGG LLTFSASC
 
 
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