ID   TETR5_ECOLX             Reviewed;         211 AA.
AC   P21337;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Tetracycline repressor protein class E;
GN   Name=tetR;
OS   Escherichia coli.
OG   Plasmid pSL1503.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-21.
RX   PubMed=3241623; DOI=10.1007/bf00331306;
RA   Tovar K., Ernst A., Hillen W.;
RT   "Identification and nucleotide sequence of the class E tet regulatory
RT   elements and operator and inducer binding of the encoded purified Tet
RT   repressor.";
RL   Mol. Gen. Genet. 215:76-80(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; X14035; CAA32196.1; -; Genomic_DNA.
DR   EMBL; M34933; AAA98409.1; -; Genomic_DNA.
DR   PIR; I77569; I77569.
DR   AlphaFoldDB; P21337; -.
DR   SMR; P21337; -.
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   Antibiotic resistance; Direct protein sequencing; DNA-binding; Magnesium;
KW   Metal-binding; Plasmid; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..211
FT                   /note="Tetracycline repressor protein class E"
FT                   /id="PRO_0000070617"
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        45
FT                   /note="V -> L (in Ref. 1; AAA98409)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   211 AA;  23585 MW;  7E9CCFBB393A881B CRC64;
     MARLSLDDVI SMALTLLDSE GLEGLTTRKL AQSLKIEQPT LYWHVRNKQT LMNMLSEAIL
     AKHHTRSAPL PTESWQQFLQ ENALSFRKAL LVHRDGARLH IGTSPTPPQF EQAEAQLRCL
     CDAGFSVEEA LFILQSISHF TLGAVLEEQA TNQIENNHVI DAAPPLLQEA FNIQARTSAE
     MAFHFGLKSL IFGFSAQLDE KKHTPIEDGN K