TRPR_ECOLI
ID TRPR_ECOLI Reviewed; 108 AA.
AC P0A881; P03032; Q2M5S4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Trp operon repressor;
GN Name=trpR; Synonyms=rtrY; OrderedLocusNames=b4393, JW4356;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7012834; DOI=10.1073/pnas.77.12.7117;
RA Gunsalus R.P., Yanofsky C.;
RT "Nucleotide sequence and expression of Escherichia coli trpR, the
RT structural gene for the trp aporepressor.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:7117-7121(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7001368; DOI=10.1093/nar/8.7.1551;
RA Singleton C.K., Roeder W.D., Bogosian G., Somerville R.L., Weith H.L.;
RT "DNA sequence of the E. coli trpR gene and prediction of the amino acid
RT sequence of Trp repressor.";
RL Nucleic Acids Res. 8:1551-1560(1980).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RA Bogosian G.;
RL Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7841459; DOI=10.3109/10425179409010185;
RA Skrypka I., Somerville R.L.;
RT "Nucleotide sequence of the Salmonella typhimurium trpR gene.";
RL DNA Seq. 4:355-360(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=1938883; DOI=10.1128/jb.173.21.6773-6782.1991;
RA Engel H., Kazemier B., Keck W.;
RT "Murein-metabolizing enzymes from Escherichia coli: sequence analysis and
RT controlled overexpression of the slt gene, which encodes the soluble lytic
RT transglycosylase.";
RL J. Bacteriol. 173:6773-6782(1991).
RN [9]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=3600756; DOI=10.1038/327591a0;
RA Zhang R.-G., Joachimiak A., Lawson C.L., Schevitz R.W., Otwinowski Z.,
RA Sigler P.B.;
RT "The crystal structure of trp aporepressor at 1.8 A shows how binding
RT tryptophan enhances DNA affinity.";
RL Nature 327:591-597(1987).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
RX PubMed=3290685; DOI=10.1038/333869a03386734;
RA Lawson C.L., Sigler P.B.;
RT "The structure of trp pseudorepressor at 1.65A shows why indole propionate
RT acts as a trp 'inducer'.";
RL Nature 333:869-871(1988).
RN [12]
RP STRUCTURE BY NMR.
RX PubMed=2207078; DOI=10.1021/bi00479a002;
RA Arrowsmith C.H., Pachter R., Altman R.B., Iyer S.B., Jardetzky O.;
RT "Sequence-specific 1H NMR assignments and secondary structure in solution
RT of Escherichia coli trp repressor.";
RL Biochemistry 29:6332-6341(1990).
RN [13]
RP STRUCTURE BY NMR.
RX PubMed=1935980; DOI=10.1111/j.1432-1033.1991.tb16344.x;
RA Arrowsmith C.H., Pachter R., Altman R.B., Jardetzky O.;
RT "The solution structures of Escherichia coli trp repressor and trp
RT aporepressor at an intermediate resolution.";
RL Eur. J. Biochem. 202:53-66(1991).
RN [14]
RP STRUCTURE BY NMR.
RX PubMed=1740124; DOI=10.1111/j.1432-1033.1992.tb16616.x;
RA Borden K.L.B., Bauer C.J., Frenkiel T.A., Beckmann P., Lane A.N.;
RT "Sequence-specific NMR assignments of the trp repressor from Escherichia
RT coli using three-dimensional 15N/1H heteronuclear techniques.";
RL Eur. J. Biochem. 204:137-146(1992).
RN [15]
RP STRUCTURE BY NMR.
RX PubMed=8433368; DOI=10.1006/jmbi.1993.1076;
RA Zhao D., Arrowsmith C.H., Jia X., Jardetzky O.;
RT "Refined solution structures of the Escherichia coli trp holo- and
RT aporepressor.";
RL J. Mol. Biol. 229:735-746(1993).
RN [16]
RP STRUCTURE BY NMR.
RX PubMed=8176748; DOI=10.1006/jmbi.1994.1317;
RA Zhang H., Zhao D., Revington M., Lee W., Jia X., Arrowsmith C.H.,
RA Jardetzky O.;
RT "The solution structures of the trp repressor-operator DNA complex.";
RL J. Mol. Biol. 238:592-614(1994).
RN [17]
RP REVIEW.
RX PubMed=2182120; DOI=10.1016/0167-4781(90)90047-6;
RA Luisi B.F., Sigler P.B.;
RT "The stereochemistry and biochemistry of the trp repressor-operator
RT complex.";
RL Biochim. Biophys. Acta 1048:113-126(1990).
CC -!- FUNCTION: This protein is an aporepressor. When complexed with L-
CC tryptophan it binds the operator region of the trp operon (5'-
CC ACTAGT-'3') and prevents the initiation of transcription. The complex
CC also regulates trp repressor biosynthesis by binding to its regulatory
CC region.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the TrpR family. {ECO:0000305}.
CC -!- CAUTION: PubMed:7841459 sequence was originally thought to originate
CC from S.typhimurium, but seems to come from an unknown E.coli strain.
CC {ECO:0000305}.
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DR EMBL; J01715; AAA72140.1; -; Genomic_DNA.
DR EMBL; L13768; AAA72134.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97289.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77346.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78382.1; -; Genomic_DNA.
DR EMBL; M69185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A03568; RPECW.
DR RefSeq; NP_418810.1; NC_000913.3.
DR RefSeq; WP_000068679.1; NZ_STEB01000033.1.
DR PDB; 1CO0; NMR; -; A/B=2-108.
DR PDB; 1JHG; X-ray; 1.30 A; A=8-108.
DR PDB; 1MI7; X-ray; 2.50 A; R=2-108.
DR PDB; 1RCS; NMR; -; A/B=4-107.
DR PDB; 1TRO; X-ray; 1.90 A; A/C/E/G=1-108.
DR PDB; 1TRR; X-ray; 2.40 A; A/B/D/E/G/H/J/K=2-108.
DR PDB; 1WRP; X-ray; 2.20 A; R=2-108.
DR PDB; 1WRS; NMR; -; R/S=4-108.
DR PDB; 1WRT; NMR; -; R/S=4-108.
DR PDB; 1ZT9; X-ray; 2.00 A; A/B/D/E=2-108.
DR PDB; 2OZ9; X-ray; 1.65 A; R=2-108.
DR PDB; 3SSW; X-ray; 1.67 A; N/R=2-108.
DR PDB; 3SSX; X-ray; 1.58 A; N/R=2-108.
DR PDB; 3WRP; X-ray; 1.80 A; A=1-108.
DR PDB; 6EJW; X-ray; 1.99 A; A/B/C/D=1-108.
DR PDB; 6EKP; X-ray; 1.46 A; A/B=1-108.
DR PDB; 6ELB; X-ray; 1.44 A; A/B=1-108.
DR PDB; 6ELF; X-ray; 1.83 A; A/B=1-108.
DR PDB; 6ELG; X-ray; 1.38 A; A/B=1-108.
DR PDB; 6ENI; X-ray; 1.10 A; A/B=1-108.
DR PDB; 6ENN; X-ray; 1.17 A; A/B=1-108.
DR PDB; 6F7F; X-ray; 2.13 A; A/B/C/D=4-106.
DR PDB; 6F7G; X-ray; 1.66 A; A/C=4-106.
DR PDB; 6F9K; X-ray; 1.40 A; A=1-107.
DR PDB; 6FAL; X-ray; 1.20 A; A/B=2-108.
DR PDB; 6ST6; X-ray; 2.05 A; A=1-105.
DR PDB; 6ST7; X-ray; 2.45 A; A=1-105.
DR PDBsum; 1CO0; -.
DR PDBsum; 1JHG; -.
DR PDBsum; 1MI7; -.
DR PDBsum; 1RCS; -.
DR PDBsum; 1TRO; -.
DR PDBsum; 1TRR; -.
DR PDBsum; 1WRP; -.
DR PDBsum; 1WRS; -.
DR PDBsum; 1WRT; -.
DR PDBsum; 1ZT9; -.
DR PDBsum; 2OZ9; -.
DR PDBsum; 3SSW; -.
DR PDBsum; 3SSX; -.
DR PDBsum; 3WRP; -.
DR PDBsum; 6EJW; -.
DR PDBsum; 6EKP; -.
DR PDBsum; 6ELB; -.
DR PDBsum; 6ELF; -.
DR PDBsum; 6ELG; -.
DR PDBsum; 6ENI; -.
DR PDBsum; 6ENN; -.
DR PDBsum; 6F7F; -.
DR PDBsum; 6F7G; -.
DR PDBsum; 6F9K; -.
DR PDBsum; 6FAL; -.
DR PDBsum; 6ST6; -.
DR PDBsum; 6ST7; -.
DR AlphaFoldDB; P0A881; -.
DR SMR; P0A881; -.
DR BioGRID; 4260801; 6.
DR BioGRID; 853194; 1.
DR DIP; DIP-48204N; -.
DR IntAct; P0A881; 3.
DR STRING; 511145.b4393; -.
DR BindingDB; P0A881; -.
DR jPOST; P0A881; -.
DR PaxDb; P0A881; -.
DR PRIDE; P0A881; -.
DR EnsemblBacteria; AAC77346; AAC77346; b4393.
DR EnsemblBacteria; BAE78382; BAE78382; BAE78382.
DR GeneID; 66671719; -.
DR GeneID; 948917; -.
DR KEGG; ecj:JW4356; -.
DR KEGG; eco:b4393; -.
DR PATRIC; fig|511145.12.peg.4542; -.
DR EchoBASE; EB1022; -.
DR eggNOG; COG2973; Bacteria.
DR HOGENOM; CLU_147939_0_0_6; -.
DR InParanoid; P0A881; -.
DR OMA; GQMSQRE; -.
DR PhylomeDB; P0A881; -.
DR BioCyc; EcoCyc:PD00423; -.
DR EvolutionaryTrace; P0A881; -.
DR PRO; PR:P0A881; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IDA:EcoCyc.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:EcoCyc.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:EcoCyc.
DR Gene3D; 1.10.1270.10; -; 1.
DR HAMAP; MF_00475; Trp_repressor; 1.
DR InterPro; IPR000831; Trp_repress.
DR InterPro; IPR013335; Trp_repress_bac.
DR InterPro; IPR010921; Trp_repressor/repl_initiator.
DR InterPro; IPR038116; TrpR-like_sf.
DR PANTHER; PTHR38025; PTHR38025; 1.
DR Pfam; PF01371; Trp_repressor; 1.
DR PIRSF; PIRSF003196; Trp_repressor; 1.
DR SUPFAM; SSF48295; SSF48295; 1.
DR TIGRFAMs; TIGR01321; TrpR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-binding; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..108
FT /note="Trp operon repressor"
FT /id="PRO_0000196494"
FT DNA_BIND 68..91
FT CONFLICT 26
FT /note="L -> V (in Ref. 4; AAA72134)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="R -> A (in Ref. 4; AAA72134)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="L -> M (in Ref. 4; AAA72134)"
FT /evidence="ECO:0000305"
FT HELIX 6..31
FT /evidence="ECO:0007829|PDB:6ENI"
FT HELIX 35..42
FT /evidence="ECO:0007829|PDB:6ENI"
FT HELIX 45..63
FT /evidence="ECO:0007829|PDB:6ENI"
FT HELIX 68..75
FT /evidence="ECO:0007829|PDB:6ENI"
FT HELIX 79..91
FT /evidence="ECO:0007829|PDB:6ENI"
FT HELIX 94..104
FT /evidence="ECO:0007829|PDB:6ENI"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:3WRP"
SQ SEQUENCE 108 AA; 12355 MW; FDFF8A60EC4FE7BE CRC64;
MAQQSPYSAA MAEQRHQEWL RFVDLLKNAY QNDLHLPLLN LMLTPDEREA LGTRVRIVEE
LLRGEMSQRE LKNELGAGIA TITRGSNSLK AAPVELRQWL EEVLLKSD
