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TETR4_SALOR
ID   TETR4_SALOR             Reviewed;         218 AA.
AC   P0ACT5; P09164;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Tetracycline repressor protein class D;
GN   Name=tetR;
OS   Salmonella ordonez.
OG   Plasmid pIP173.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BM2000;
RX   PubMed=8384294; DOI=10.1007/bf00282811;
RA   Allard J.D., Gibson M.L., Vu L.H., Nguyen T.T., Bertrand K.P.;
RT   "Nucleotide sequence of class D tetracycline resistance genes from
RT   Salmonella ordonez.";
RL   Mol. Gen. Genet. 237:301-305(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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
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DR   EMBL; X65876; CAA46707.1; -; Genomic_DNA.
DR   PIR; S30287; S30287.
DR   AlphaFoldDB; P0ACT5; -.
DR   SMR; P0ACT5; -.
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   3: Inferred from homology;
KW   Antibiotic resistance; DNA-binding; Magnesium; Metal-binding; Plasmid;
KW   Repressor; Transcription; Transcription regulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..218
FT                   /note="Tetracycline repressor protein class D"
FT                   /id="PRO_0000070616"
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
 
 
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