TTGR_PSEPT
ID TTGR_PSEPT Reviewed; 210 AA.
AC Q9AIU0; I7B485;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=HTH-type transcriptional regulator TtgR;
DE AltName: Full=Toluene efflux pump ttgABC operon repressor;
GN Name=ttgR; OrderedLocusNames=T1E_0244;
OS Pseudomonas putida (strain DOT-T1E).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1196325;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=DOT-T1E;
RX PubMed=11251828; DOI=10.1046/j.1365-2958.2001.02310.x;
RA Duque E., Segura A., Mosqueda G., Ramos J.L.;
RT "Global and cognate regulators control the expression of the organic
RT solvent efflux pumps TtgABC and TtgDEF of Pseudomonas putida.";
RL Mol. Microbiol. 39:1100-1106(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DOT-T1E;
RX PubMed=23815283; DOI=10.1111/1751-7915.12061;
RA Udaondo Z., Molina L., Daniels C., Gomez M.J., Molina-Henares M.A.,
RA Matilla M.A., Roca A., Fernandez M., Duque E., Segura A., Ramos J.L.;
RT "Metabolic potential of the organic-solvent tolerant Pseudomonas putida
RT DOT-T1E deduced from its annotated genome.";
RL Microb. Biotechnol. 6:598-611(2013).
RN [3]
RP DNA-BINDING, AND INDUCTION BY ANTIBIOTICS.
RC STRAIN=DOT-T1E;
RX PubMed=14506010; DOI=10.1128/aac.47.10.3067-3072.2003;
RA Teran W., Felipe A., Segura A., Rojas A., Ramos J.L., Gallegos M.T.;
RT "Antibiotic-dependent induction of Pseudomonas putida DOT-T1E TtgABC efflux
RT pump is mediated by the drug binding repressor TtgR.";
RL Antimicrob. Agents Chemother. 47:3067-3072(2003).
CC -!- FUNCTION: Represses expression from the ttgABC operon promoter and its
CC own expression. Binds to a promoter region between the divergently
CC transcribed ttgR and ttgABC genes/operons; in the presence of
CC chloramphenicol or tetracycline this binding no longer occurs and ttgR
CC and ttgABC are derepressed. This suggests that TtgR binds these
CC antibiotics. {ECO:0000269|PubMed:11251828}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- INDUCTION: Induced 4- to 8-fold in the presence of toluene; this is
CC controlled by TtgX, a possible efflux pump global regulator. Induced by
CC chloramphenicol and probably by tetracycline.
CC {ECO:0000269|PubMed:14506010}.
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; AF238479; AAK15050.1; -; Genomic_DNA.
DR EMBL; CP003734; AFO46103.1; -; Genomic_DNA.
DR PDB; 2UXH; X-ray; 2.40 A; A/B=1-210.
DR PDB; 2UXI; X-ray; 2.50 A; A/B=1-210.
DR PDB; 2UXO; X-ray; 2.70 A; A/B=1-210.
DR PDB; 2UXP; X-ray; 2.70 A; A/B=1-210.
DR PDB; 2UXU; X-ray; 2.30 A; A/B=1-210.
DR PDB; 2XDN; X-ray; 2.20 A; A/B/C/D=1-210.
DR PDB; 7K1A; X-ray; 1.75 A; A/B=1-210.
DR PDB; 7K1C; X-ray; 1.90 A; A/B=1-210.
DR PDB; 7KD8; X-ray; 1.71 A; A/B/C/D=1-210.
DR PDBsum; 2UXH; -.
DR PDBsum; 2UXI; -.
DR PDBsum; 2UXO; -.
DR PDBsum; 2UXP; -.
DR PDBsum; 2UXU; -.
DR PDBsum; 2XDN; -.
DR PDBsum; 7K1A; -.
DR PDBsum; 7K1C; -.
DR PDBsum; 7KD8; -.
DR AlphaFoldDB; Q9AIU0; -.
DR SMR; Q9AIU0; -.
DR DrugBank; DB03467; Naringenin.
DR DrugBank; DB07810; Phloretin.
DR DrugBank; DB04216; Quercetin.
DR PRIDE; Q9AIU0; -.
DR EnsemblBacteria; AFO46103; AFO46103; T1E_0244.
DR KEGG; ppx:T1E_0244; -.
DR PATRIC; fig|1196325.3.peg.245; -.
DR HOGENOM; CLU_069356_12_3_6; -.
DR EvolutionaryTrace; Q9AIU0; -.
DR PRO; PR:Q9AIU0; -.
DR Proteomes; UP000006503; Chromosome.
DR GO; GO:0032993; C:protein-DNA complex; IMP:CollecTF.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IMP:CollecTF.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IMP:CollecTF.
DR InterPro; IPR023772; DNA-bd_HTH_TetR-type_CS.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001647; HTH_TetR.
DR InterPro; IPR036271; Tet_transcr_reg_TetR-rel_C_sf.
DR InterPro; IPR013572; Tscrpt_reg_MAATS_C.
DR Pfam; PF08361; TetR_C_2; 1.
DR Pfam; PF00440; TetR_N; 1.
DR PRINTS; PR00455; HTHTETR.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF48498; SSF48498; 1.
DR PROSITE; PS01081; HTH_TETR_1; 1.
DR PROSITE; PS50977; HTH_TETR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..210
FT /note="HTH-type transcriptional regulator TtgR"
FT /id="PRO_0000070623"
FT DOMAIN 10..70
FT /note="HTH tetR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
FT DNA_BIND 33..52
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
FT HELIX 5..27
FT /evidence="ECO:0007829|PDB:7KD8"
FT TURN 28..31
FT /evidence="ECO:0007829|PDB:2UXU"
FT HELIX 34..41
FT /evidence="ECO:0007829|PDB:7KD8"
FT HELIX 47..51
FT /evidence="ECO:0007829|PDB:7KD8"
FT HELIX 55..65
FT /evidence="ECO:0007829|PDB:7KD8"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:7KD8"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:7KD8"
FT HELIX 85..102
FT /evidence="ECO:0007829|PDB:7KD8"
FT HELIX 104..115
FT /evidence="ECO:0007829|PDB:7KD8"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:7K1A"
FT HELIX 125..150
FT /evidence="ECO:0007829|PDB:7KD8"
FT HELIX 160..180
FT /evidence="ECO:0007829|PDB:7KD8"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:7KD8"
FT TURN 187..190
FT /evidence="ECO:0007829|PDB:7KD8"
FT HELIX 191..204
FT /evidence="ECO:0007829|PDB:7KD8"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:7KD8"
SQ SEQUENCE 210 AA; 23854 MW; 237211F9046B9F9E CRC64;
MVRRTKEEAQ ETRAQIIEAA ERAFYKRGVA RTTLADIAEL AGVTRGAIYW HFNNKAELVQ
ALLDSLHETH DHLARASESE DEVDPLGCMR KLLLQVFNEL VLDARTRRIN EILHHKCEFT
DDMCEIRQQR QSAVLDCHKG ITLALANAVR RGQLPGELDA ERAAVAMFAY VDGLIRRWLL
LPDSVDLLGD VEKWVDTGLD MLRLSPALRK
