TETR8_PHODP
ID TETR8_PHODP Reviewed; 218 AA.
AC P51562;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Tetracycline repressor protein class H;
GN Name=tetR;
OS Photobacterium damsela subsp. piscicida (Pasteurella piscicida).
OG Plasmid pSP9351.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=38294;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8052160; DOI=10.1111/j.1348-0421.1994.tb01741.x;
RA Kim E.H., Aoki T.;
RT "The transposon-like structure of IS26-tetracycline, and kanamycin
RT resistance determinant derived from transferable R plasmid of fish
RT pathogen, Pasteurella piscicida.";
RL Microbiol. Immunol. 38:31-38(1994).
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; D16172; BAA03720.1; -; Genomic_DNA.
DR RefSeq; WP_000113282.1; NZ_LC225353.1.
DR RefSeq; YP_003023971.1; NC_012919.1.
DR RefSeq; YP_908416.1; NC_008612.1.
DR RefSeq; YP_908600.1; NC_008613.1.
DR AlphaFoldDB; P51562; -.
DR SMR; P51562; -.
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 2: Evidence at transcript level;
KW Antibiotic resistance; DNA-binding; Magnesium; Metal-binding; Plasmid;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..218
FT /note="Tetracycline repressor protein class H"
FT /id="PRO_0000070620"
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"
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
