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Database: UniProt
Entry: P03038
LinkDB: P03038
Original site: P03038 
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   05-DEC-2018, entry version 120.
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
RT   gene 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:
RT   nucleotide sequence analysis.";
RL   Nucleic Acids Res. 11:6089-6105(1983).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100.
RX   PubMed=3208760;
RA   Altschmied L., Baumeister R., Pfleiderer K., Hillen W.;
RT   "A threonine to alanine exchange at position 40 of Tet repressor
RT   alters the recognition of the sixth base pair of tet operator from GC
RT   to AT.";
RL   EMBO J. 7:4011-4017(1988).
CC   -!- FUNCTION: TetR is the repressor of the tetracycline resistance
CC       element; its N-terminal region forms a helix-turn-helix structure
CC       and binds DNA. Binding of tetracycline to TetR reduces the
CC       repressor affinity for the tetracycline resistance gene (tetA)
CC       promoter operator sites.
CC   -!- INDUCTION: By the [Mg-tetracycline]+ complex.
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_UDCU01000030.1.
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   ProteinModelPortal; P03038; -.
DR   SMR; P03038; -.
DR   GeneID; 13906581; -.
DR   GeneID; 20466875; -.
DR   GeneID; 2716476; -.
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   InterPro; IPR039419; TetR_trans_reg.
DR   PANTHER; PTHR30328; PTHR30328; 1.
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;
KW   Metal-binding; Plasmid; Repressor; Transcription;
KW   Transcription regulation; Transposable element.
FT   CHAIN         1    216       Tetracycline repressor protein class A
FT                                from transposon 1721.
FT                                /FTId=PRO_0000070612.
FT   DOMAIN        3     63       HTH tetR-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00335}.
FT   DNA_BIND     26     45       H-T-H motif. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00335}.
FT   METAL       100    100       Magnesium [Mg-tetracycline].
FT                                {ECO:0000250}.
FT   SITE         64     64       Involved in binding magnesium-
FT                                tetracycline complex. {ECO:0000250}.
FT   CONFLICT     65     66       TH -> ST (in Ref. 3; CAA24908).
FT                                {ECO:0000305}.
FT   CONFLICT     80     80       I -> T (in Ref. 3; CAA24908).
FT                                {ECO:0000305}.
FT   CONFLICT    154    155       DA -> ES (in Ref. 3; CAA24908).
FT                                {ECO:0000305}.
FT   HELIX         7     24       {ECO:0000244|PDB:5MRU}.
FT   HELIX        27     34       {ECO:0000244|PDB:5MRU}.
FT   HELIX        48     63       {ECO:0000244|PDB:5MRU}.
FT   HELIX        75     91       {ECO:0000244|PDB:5MRU}.
FT   HELIX        96    100       {ECO:0000244|PDB:5MRU}.
FT   HELIX       107    123       {ECO:0000244|PDB:5MRU}.
FT   HELIX       127    153       {ECO:0000244|PDB:5MRU}.
FT   TURN        154    156       {ECO:0000244|PDB:5MRU}.
FT   HELIX       183    199       {ECO:0000244|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
//
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