TETR2_ECOLX
ID TETR2_ECOLX Reviewed; 207 AA.
AC P04483;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Tetracycline repressor protein class B from transposon Tn10;
GN Name=tetR;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6330687; DOI=10.1093/nar/12.12.4849;
RA Postle K., Nguyen T.T., Bertrand K.P.;
RT "Nucleotide sequence of the repressor gene of the TN10 tetracycline
RT resistance determinant.";
RL Nucleic Acids Res. 12:4849-4863(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100.
RX PubMed=3208760; DOI=10.1002/j.1460-2075.1988.tb03290.x;
RA Altschmied L., Baumeister R., Pfleiderer K., Hillen W.;
RT "A threonine to alanine exchange at position 40 of Tet repressor alters the
RT recognition of the sixth base pair of tet operator from GC to AT.";
RL EMBO J. 7:4011-4017(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
RX PubMed=6311683; DOI=10.1016/0378-1119(83)90046-x;
RA Bertrand K.P., Postle K., Wray L.V. Jr., Reznikoff W.S.;
RT "Overlapping divergent promoters control expression of Tn10 tetracycline
RT resistance.";
RL Gene 23:149-156(1983).
RN [4]
RP MUTAGENESIS.
RX PubMed=3062183; DOI=10.1016/0022-2836(88)90120-9;
RA Smith L.D., Bertrand K.P.;
RT "Mutations in the Tn10 tet repressor that interfere with induction.
RT Location of the tetracycline-binding domain.";
RL J. Mol. Biol. 203:949-959(1988).
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.
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DR EMBL; X00694; CAA25291.1; -; Genomic_DNA.
DR EMBL; J01830; AAB59093.1; -; Genomic_DNA.
DR PIR; A03576; RPECTN.
DR RefSeq; WP_000088605.1; NZ_WVVR01000059.1.
DR RefSeq; YP_001096449.1; NC_009133.1.
DR PDB; 2NS7; X-ray; 2.40 A; A/B/C/D=1-187.
DR PDB; 2NS8; X-ray; 2.55 A; A/B/C/D=1-187.
DR PDB; 2VKV; X-ray; 1.74 A; A=1-50.
DR PDB; 2XGC; X-ray; 2.15 A; A/B=1-50.
DR PDB; 2XGD; X-ray; 2.25 A; A=1-50.
DR PDB; 2XGE; X-ray; 2.14 A; A/B=1-50.
DR PDB; 3FK6; X-ray; 2.10 A; A/B=1-50.
DR PDB; 3FK7; X-ray; 2.06 A; A/B=1-50.
DR PDB; 3ZQF; X-ray; 2.56 A; A=1-187.
DR PDB; 3ZQG; X-ray; 2.45 A; A=1-187.
DR PDB; 3ZQH; X-ray; 1.60 A; A=1-187.
DR PDB; 3ZQI; X-ray; 1.50 A; A/B=1-187.
DR PDB; 4AC0; X-ray; 2.45 A; A=2-203.
DR PDB; 6SY4; X-ray; 2.69 A; A/B=1-203.
DR PDB; 6SY6; X-ray; 2.90 A; A/B=1-203.
DR PDBsum; 2NS7; -.
DR PDBsum; 2NS8; -.
DR PDBsum; 2VKV; -.
DR PDBsum; 2XGC; -.
DR PDBsum; 2XGD; -.
DR PDBsum; 2XGE; -.
DR PDBsum; 3FK6; -.
DR PDBsum; 3FK7; -.
DR PDBsum; 3ZQF; -.
DR PDBsum; 3ZQG; -.
DR PDBsum; 3ZQH; -.
DR PDBsum; 3ZQI; -.
DR PDBsum; 4AC0; -.
DR PDBsum; 6SY4; -.
DR PDBsum; 6SY6; -.
DR AlphaFoldDB; P04483; -.
DR SMR; P04483; -.
DR GeneID; 66619376; -.
DR OMA; SALYWHF; -.
DR OrthoDB; 1437290at2; -.
DR EvolutionaryTrace; P04483; -.
DR PRO; PR:P04483; -.
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; DNA-binding; Magnesium; Metal-binding;
KW Repressor; Transcription; Transcription regulation; Transposable element.
FT CHAIN 1..207
FT /note="Tetracycline repressor protein class B from
FT transposon Tn10"
FT /id="PRO_0000070613"
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:0000250|UniProtKB:P0ACT4"
FT BINDING 82
FT /ligand="tetracycline"
FT /ligand_id="ChEBI:CHEBI:77932"
FT /evidence="ECO:0000250|UniProtKB:P0ACT4"
FT BINDING 100
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0ACT4"
FT MUTAGEN 64
FT /note="H->Y: 1000-fold reduction of affinity for
FT tetracycline."
FT /evidence="ECO:0000269|PubMed:3062183"
FT MUTAGEN 82
FT /note="N->H: 100-fold reduction of affinity for
FT tetracycline."
FT /evidence="ECO:0000269|PubMed:3062183"
FT MUTAGEN 103
FT /note="T->I: <10-fold reduction of affinity for
FT tetracycline."
FT /evidence="ECO:0000269|PubMed:3062183"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:2XGE"
FT HELIX 6..24
FT /evidence="ECO:0007829|PDB:3ZQI"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:3ZQI"
FT HELIX 38..44
FT /evidence="ECO:0007829|PDB:3ZQI"
FT HELIX 48..63
FT /evidence="ECO:0007829|PDB:3ZQI"
FT HELIX 75..91
FT /evidence="ECO:0007829|PDB:3ZQI"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:3ZQI"
FT HELIX 107..120
FT /evidence="ECO:0007829|PDB:3ZQI"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:3ZQF"
FT HELIX 127..157
FT /evidence="ECO:0007829|PDB:3ZQI"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:2NS8"
FT HELIX 168..180
FT /evidence="ECO:0007829|PDB:3ZQI"
FT HELIX 182..187
FT /evidence="ECO:0007829|PDB:3ZQI"
SQ SEQUENCE 207 AA; 23355 MW; A9FD75972352CC80 CRC64;
MSRLDKSKVI NSALELLNEV GIEGLTTRKL AQKLGVEQPT LYWHVKNKRA LLDALAIEML
DRHHTHFCPL EGESWQDFLR NNAKSFRCAL LSHRDGAKVH LGTRPTEKQY ETLENQLAFL
CQQGFSLENA LYALSAVGHF TLGCVLEDQE HQVAKEERET PTTDSMPPLL RQAIELFDHQ
GAEPAFLFGL ELIICGLEKQ LKCESGS
