TETR4_ECOLX
ID TETR4_ECOLX Reviewed; 218 AA.
AC P0ACT4; P09164;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Tetracycline repressor protein class D;
GN Name=tetR;
OS Escherichia coli.
OG Plasmid RA1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=J53-1;
RX PubMed=6093049; DOI=10.1093/nar/12.20.7693;
RA Unger B., Klock G., Hillen W.;
RT "Nucleotide sequence of the repressor gene of the RA1 tetracycline
RT resistance determinant: structural and functional comparison with three
RT related Tet repressor genes.";
RL Nucleic Acids Res. 12:7693-7703(1984).
RN [2] {ECO:0007744|PDB:2TRT}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
RP TETRACYCLINE, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8153629; DOI=10.1126/science.8153629;
RA Hinrichs W., Kisker C., Duevel C., Mueller A., Tovar K., Hillen W.,
RA Saenger W.;
RT "Structure of the Tet repressor-tetracycline complex and regulation of
RT antibiotic resistance.";
RL Science 264:418-420(1994).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=9642048; DOI=10.1006/jmbi.1998.1775;
RA Orth P., Cordes F., Schnappinger D., Hillen W., Saenger W., Hinrichs W.;
RT "Conformational changes of the Tet repressor induced by tetracycline
RT trapping.";
RL J. Mol. Biol. 279:439-447(1998).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=9890898; DOI=10.1021/bi9816610;
RA Orth P., Saenger W., Hinrichs W.;
RT "Tetracycline-chelated Mg2+ ion initiates helix unwinding in Tet repressor
RT induction.";
RL Biochemistry 38:191-198(1999).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=9878420; DOI=10.1006/jmbi.1998.2290;
RA Orth P., Schnappinger D., Sum P.-E., Ellestad G.A., Hillen W., Saenger W.,
RA Hinrichs W.;
RT "Crystal structure of the tet repressor in complex with a novel
RT tetracycline, 9-(N,N-dimethylglycylamido)-6-demethyl-6-deoxy-
RT tetracycline.";
RL J. Mol. Biol. 285:455-461(1999).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 1-208.
RX PubMed=10700280; DOI=10.1038/73324;
RA Orth P., Schnappinger D., Hillen W., Saenger W., Hinrichs W.;
RT "Structural basis of gene regulation by the tetracycline inducible Tet
RT repressor-operator system.";
RL Nat. Struct. Biol. 7:215-219(2000).
CC -!- FUNCTION: TetR is the repressor of the tetracycline resistance element;
CC its N-terminal region forms a helix-turn-helix structure and binds DNA.
CC Binding of tetracycline to TetR reduces the repressor affinity for the
CC tetracycline resistance gene (tetA) promoter operator sites.
CC -!- SUBUNIT: Homodimer.
CC -!- INDUCTION: By the [Mg-tetracycline]+ complex.
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DR EMBL; X01083; CAA25561.1; -; Genomic_DNA.
DR PIR; S07359; S07359.
DR RefSeq; WP_000113282.1; NZ_WSXE01000114.1.
DR RefSeq; YP_002995714.1; NC_012886.1.
DR RefSeq; YP_007349483.1; NC_020086.1.
DR PDB; 1A6I; X-ray; 2.40 A; A=6-218.
DR PDB; 1BJZ; X-ray; 2.20 A; A=3-208.
DR PDB; 1ORK; X-ray; 2.40 A; A=3-208.
DR PDB; 1QPI; X-ray; 2.50 A; A=4-206.
DR PDB; 2FJ1; X-ray; 2.20 A; A=2-208.
DR PDB; 2NS7; X-ray; 2.40 A; A/B/C/D=188-208.
DR PDB; 2NS8; X-ray; 2.55 A; A/B/C/D=188-208.
DR PDB; 2O7O; X-ray; 1.89 A; A=2-208.
DR PDB; 2TCT; X-ray; 2.10 A; A=2-208.
DR PDB; 2TRT; X-ray; 2.50 A; A=2-218.
DR PDB; 2VKE; X-ray; 1.62 A; A=3-208.
DR PDB; 2VKV; X-ray; 1.74 A; A=51-208.
DR PDB; 2X6O; X-ray; 2.30 A; A=3-208.
DR PDB; 2X9D; X-ray; 2.51 A; A=3-208.
DR PDB; 2XB5; X-ray; 2.50 A; A=2-208.
DR PDB; 2XGC; X-ray; 2.15 A; A/B=51-208.
DR PDB; 2XGD; X-ray; 2.25 A; A=51-208.
DR PDB; 2XGE; X-ray; 2.14 A; A/B=51-208.
DR PDB; 2XPU; X-ray; 1.55 A; A=3-208.
DR PDB; 2XPV; X-ray; 1.49 A; A=3-208.
DR PDB; 2XPW; X-ray; 1.44 A; A=3-208.
DR PDB; 2XRL; X-ray; 1.85 A; A=3-208.
DR PDB; 3FK6; X-ray; 2.10 A; A/B=51-208.
DR PDB; 3FK7; X-ray; 2.06 A; A/B=51-208.
DR PDB; 3ZQF; X-ray; 2.56 A; A=188-208.
DR PDB; 3ZQG; X-ray; 2.45 A; A=188-208.
DR PDB; 3ZQH; X-ray; 1.60 A; A=188-208.
DR PDB; 3ZQI; X-ray; 1.50 A; A/B=188-208.
DR PDB; 4ABZ; X-ray; 1.89 A; A=3-208.
DR PDB; 4AUX; X-ray; 2.25 A; A=2-208.
DR PDB; 4B1R; X-ray; 1.95 A; A=3-208.
DR PDB; 4B3A; X-ray; 1.70 A; A=3-208.
DR PDB; 4D7M; X-ray; 1.75 A; A=3-208.
DR PDB; 4D7N; X-ray; 1.89 A; A=3-208.
DR PDB; 4V2F; X-ray; 2.40 A; A=3-208.
DR PDB; 4V2G; X-ray; 2.70 A; A/B=3-208.
DR PDB; 5FKK; X-ray; 1.75 A; A/B=3-208.
DR PDB; 5FKL; X-ray; 1.90 A; A=3-208.
DR PDB; 5FKM; X-ray; 1.63 A; A=3-208.
DR PDB; 5FKN; X-ray; 1.80 A; A/B=3-208.
DR PDB; 5FKO; X-ray; 1.85 A; A=3-208.
DR PDB; 6FPL; X-ray; 1.60 A; A=2-208.
DR PDB; 6FPM; X-ray; 1.85 A; A=2-208.
DR PDB; 6FTS; X-ray; 2.00 A; A=3-208.
DR PDB; 6QJW; X-ray; 2.10 A; A=2-208.
DR PDB; 6QJX; X-ray; 2.10 A; A=2-208.
DR PDB; 6RBL; X-ray; 1.90 A; A=2-208.
DR PDB; 6RBM; X-ray; 2.05 A; A=2-208.
DR PDB; 6RCR; X-ray; 2.05 A; A=2-208.
DR PDB; 6RGX; X-ray; 1.80 A; A/B=3-208.
DR PDB; 6YR1; X-ray; 2.30 A; AAA=3-208.
DR PDB; 6YR2; X-ray; 1.95 A; AAA/BBB=2-208.
DR PDBsum; 1A6I; -.
DR PDBsum; 1BJZ; -.
DR PDBsum; 1ORK; -.
DR PDBsum; 1QPI; -.
DR PDBsum; 2FJ1; -.
DR PDBsum; 2NS7; -.
DR PDBsum; 2NS8; -.
DR PDBsum; 2O7O; -.
DR PDBsum; 2TCT; -.
DR PDBsum; 2TRT; -.
DR PDBsum; 2VKE; -.
DR PDBsum; 2VKV; -.
DR PDBsum; 2X6O; -.
DR PDBsum; 2X9D; -.
DR PDBsum; 2XB5; -.
DR PDBsum; 2XGC; -.
DR PDBsum; 2XGD; -.
DR PDBsum; 2XGE; -.
DR PDBsum; 2XPU; -.
DR PDBsum; 2XPV; -.
DR PDBsum; 2XPW; -.
DR PDBsum; 2XRL; -.
DR PDBsum; 3FK6; -.
DR PDBsum; 3FK7; -.
DR PDBsum; 3ZQF; -.
DR PDBsum; 3ZQG; -.
DR PDBsum; 3ZQH; -.
DR PDBsum; 3ZQI; -.
DR PDBsum; 4ABZ; -.
DR PDBsum; 4AUX; -.
DR PDBsum; 4B1R; -.
DR PDBsum; 4B3A; -.
DR PDBsum; 4D7M; -.
DR PDBsum; 4D7N; -.
DR PDBsum; 4V2F; -.
DR PDBsum; 4V2G; -.
DR PDBsum; 5FKK; -.
DR PDBsum; 5FKL; -.
DR PDBsum; 5FKM; -.
DR PDBsum; 5FKN; -.
DR PDBsum; 5FKO; -.
DR PDBsum; 6FPL; -.
DR PDBsum; 6FPM; -.
DR PDBsum; 6FTS; -.
DR PDBsum; 6QJW; -.
DR PDBsum; 6QJX; -.
DR PDBsum; 6RBL; -.
DR PDBsum; 6RBM; -.
DR PDBsum; 6RCR; -.
DR PDBsum; 6RGX; -.
DR PDBsum; 6YR1; -.
DR PDBsum; 6YR2; -.
DR AlphaFoldDB; P0ACT4; -.
DR SASBDB; P0ACT4; -.
DR SMR; P0ACT4; -.
DR EvolutionaryTrace; P0ACT4; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR InterPro; IPR023772; DNA-bd_HTH_TetR-type_CS.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001647; HTH_TetR.
DR InterPro; IPR004111; Repressor_TetR_C.
DR InterPro; IPR003012; Tet_transcr_reg_TetR.
DR InterPro; IPR036271; Tet_transcr_reg_TetR-rel_C_sf.
DR Pfam; PF02909; TetR_C_1; 1.
DR Pfam; PF00440; TetR_N; 1.
DR PRINTS; PR00455; HTHTETR.
DR PRINTS; PR00400; TETREPRESSOR.
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; Antibiotic resistance; Direct protein sequencing;
KW DNA-binding; Magnesium; Metal-binding; Plasmid; Repressor; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..218
FT /note="Tetracycline repressor protein class D"
FT /id="PRO_0000070615"
FT DOMAIN 3..63
FT /note="HTH tetR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
FT DNA_BIND 26..45
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
FT BINDING 64
FT /ligand="tetracycline"
FT /ligand_id="ChEBI:CHEBI:77932"
FT /evidence="ECO:0000269|PubMed:8153629,
FT ECO:0007744|PDB:2TRT"
FT BINDING 82
FT /ligand="tetracycline"
FT /ligand_id="ChEBI:CHEBI:77932"
FT /evidence="ECO:0000269|PubMed:8153629,
FT ECO:0007744|PDB:2TRT"
FT BINDING 100
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:8153629,
FT ECO:0007744|PDB:2TRT"
FT HELIX 6..24
FT /evidence="ECO:0007829|PDB:2XPW"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:2XPW"
FT HELIX 38..44
FT /evidence="ECO:0007829|PDB:2XPW"
FT HELIX 48..63
FT /evidence="ECO:0007829|PDB:2XPW"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:2XGE"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:2XGE"
FT HELIX 75..91
FT /evidence="ECO:0007829|PDB:2XPW"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:2XPW"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:2XGE"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:2XPW"
FT HELIX 110..122
FT /evidence="ECO:0007829|PDB:2XPW"
FT HELIX 127..156
FT /evidence="ECO:0007829|PDB:2XPW"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:2XPW"
FT HELIX 168..178
FT /evidence="ECO:0007829|PDB:2XPW"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:2XPV"
FT HELIX 183..203
FT /evidence="ECO:0007829|PDB:2XPW"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:2XGC"
SQ SEQUENCE 218 AA; 24419 MW; B1F0F0EE6B4CF991 CRC64;
MARLNRESVI DAALELLNET GIDGLTTRKL AQKLGIEQPT LYWHVKNKRA LLDALAVEIL
ARHHDYSLPA AGESWQSFLR NNAMSFRRAL LRYRDGAKVH LGTRPDEKQY DTVETQLRFM
TENGFSLRDG LYAISAVSHF TLGAVLEQQE HTAALTDRPA APDENLPPLL REALQIMDSD
DGEQAFLHGL ESLIRGFEVQ LTALLQIVGG DKLIIPFC
