TETR1_ECOLX
ID TETR1_ECOLX Reviewed; 216 AA.
AC P03038;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Tetracycline repressor protein class A from transposon 1721;
GN Name=tetR;
OS Escherichia coli.
OG Plasmid RP1, and Plasmid IncP-alpha RP4.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TRANSPOSON=Tn1721;
RX PubMed=1312499; DOI=10.1016/0378-1119(92)90597-i;
RA Allmeier H., Cresnar B., Greck M., Schmitt R.;
RT "Complete nucleotide sequence of Tn1721: gene organization and a novel gene
RT product with features of a chemotaxis protein.";
RL Gene 111:11-20(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=IncP-alpha RP4;
RA Trueman P., Sharpe G.S., Barth P.T.;
RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=RP1; TRANSPOSON=Tn1721;
RX PubMed=6310527; DOI=10.1093/nar/11.17.6089;
RA Waters S.H., Rogowsky P., Grinsted J., Altenbuchner J., Schmitt R.;
RT "The tetracycline resistance determinants of RP1 and Tn1721: nucleotide
RT sequence analysis.";
RL Nucleic Acids Res. 11:6089-6105(1983).
RN [4]
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).
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 -!- INDUCTION: By the [Mg-tetracycline]+ complex.
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DR EMBL; X61367; CAA43642.1; -; Genomic_DNA.
DR EMBL; X75761; CAA53388.1; -; Genomic_DNA.
DR EMBL; X00006; CAA24908.1; -; Genomic_DNA.
DR PIR; A03574; RPECR1.
DR PIR; JQ1478; JQ1478.
DR RefSeq; NP_957552.1; NC_005327.1.
DR RefSeq; WP_000164043.1; NZ_WWEL01000009.1.
DR RefSeq; YP_006953646.1; NC_019082.1.
DR RefSeq; YP_009060102.1; NC_024956.1.
DR PDB; 5MRU; X-ray; 2.55 A; A=1-216.
DR PDBsum; 5MRU; -.
DR AlphaFoldDB; P03038; -.
DR SMR; P03038; -.
DR GeneID; 58463758; -.
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 Plasmid; Repressor; Transcription; Transcription regulation;
KW Transposable element.
FT CHAIN 1..216
FT /note="Tetracycline repressor protein class A from
FT transposon 1721"
FT /id="PRO_0000070612"
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 CONFLICT 65..66
FT /note="TH -> ST (in Ref. 3; CAA24908)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="I -> T (in Ref. 3; CAA24908)"
FT /evidence="ECO:0000305"
FT CONFLICT 154..155
FT /note="DA -> ES (in Ref. 3; CAA24908)"
FT /evidence="ECO:0000305"
FT HELIX 7..24
FT /evidence="ECO:0007829|PDB:5MRU"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:5MRU"
FT HELIX 48..63
FT /evidence="ECO:0007829|PDB:5MRU"
FT HELIX 75..91
FT /evidence="ECO:0007829|PDB:5MRU"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:5MRU"
FT HELIX 107..123
FT /evidence="ECO:0007829|PDB:5MRU"
FT HELIX 127..153
FT /evidence="ECO:0007829|PDB:5MRU"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:5MRU"
FT HELIX 183..199
FT /evidence="ECO:0007829|PDB:5MRU"
SQ SEQUENCE 216 AA; 23320 MW; 4C19319986221AF5 CRC64;
MTKLQPNTVI RAALDLLNEV GVDGLTTRKL AERLGVQQPA LYWHFRNKRA LLDALAEAML
AENHTHSVPR ADDDWRSFLI GNARSFRQAL LAYRDGARIH AGTRPGAPQM ETADAQLRFL
CEAGFSAGDA VNALMTISYF TVGAVLEEQA GDSDAGERGG TVEQAPLSPL LRAAIDAFDE
AGPDAAFEQG LAVIVDGLAK RRLVVRNVEG PRKGDD
