TETR8_PASMD
ID TETR8_PASMD Reviewed; 207 AA.
AC P51561;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Tetracycline repressor protein class H;
GN Name=tetR;
OS Pasteurella multocida.
OG Plasmid pVM111.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=747;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=P2862;
RX PubMed=8109938; DOI=10.1128/aac.37.12.2699;
RA Hansen L.M., McMurry L.M., Levy S.B., Hirsh D.C.;
RT "A new tetracycline resistance determinant, Tet H, from Pasteurella
RT multocida specifying active efflux of tetracycline.";
RL Antimicrob. Agents Chemother. 37:2699-2705(1993).
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; U00792; AAC43249.1; -; Unassigned_DNA.
DR PDB; 2VPR; X-ray; 2.49 A; A=1-207.
DR PDBsum; 2VPR; -.
DR AlphaFoldDB; P51561; -.
DR SMR; P51561; -.
DR EvolutionaryTrace; P51561; -.
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.
FT CHAIN 1..207
FT /note="Tetracycline repressor protein class H"
FT /id="PRO_0000070619"
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 HELIX 6..24
FT /evidence="ECO:0007829|PDB:2VPR"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:2VPR"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:2VPR"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:2VPR"
FT HELIX 48..63
FT /evidence="ECO:0007829|PDB:2VPR"
FT HELIX 75..92
FT /evidence="ECO:0007829|PDB:2VPR"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:2VPR"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:2VPR"
FT HELIX 110..123
FT /evidence="ECO:0007829|PDB:2VPR"
FT HELIX 127..153
FT /evidence="ECO:0007829|PDB:2VPR"
FT HELIX 170..181
FT /evidence="ECO:0007829|PDB:2VPR"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:2VPR"
FT HELIX 185..204
FT /evidence="ECO:0007829|PDB:2VPR"
SQ SEQUENCE 207 AA; 23156 MW; 1D9F9FEA975503AF CRC64;
MAKLDKEQVI DDALILLNEV GIEGLTTRNV AQKIGVEQPT LYWHVKNKRA LLDALAETIL
QKHHHHVLPL PNETWQDFLR NNAKSFRQAL LMYRDGGKIH AGTRPSESQF ETSEQQLQFL
CDAGFSLSQA VYALSSIAHF TLGSVLETQE HQESQKEREK VETDTVAYPP LLTQAVAIMD
SDNGDAAFLF VLDVMISGLE TVLKSAK
