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P0A881

- TRPR_ECOLI

UniProt

P0A881 - TRPR_ECOLI

Protein

Trp operon repressor

Gene

trpR

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    This protein is an aporepressor. When complexed with L-tryptophan it binds the operator region of the trp operon (5'-ACTAGT-'3') and prevents the initiation of transcription. The complex also regulates trp repressor biosynthesis by binding to its regulatory region.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi68 – 9124Add
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: EcoCyc
    2. sequence-specific DNA binding Source: EcoCyc
    3. sequence-specific DNA binding transcription factor activity Source: InterPro

    GO - Biological processi

    1. negative regulation of transcription, DNA-templated Source: UniProtKB-HAMAP
    2. regulation of transcription, DNA-templated Source: EcoCyc
    3. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:PD00423.
    ECOL316407:JW4356-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trp operon repressor
    Gene namesi
    Name:trpR
    Synonyms:rtrY
    Ordered Locus Names:b4393, JW4356
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11029. trpR.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 108107Trp operon repressorPRO_0000196494Add
    BLAST

    Proteomic databases

    PaxDbiP0A881.
    PRIDEiP0A881.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A881.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    DIPiDIP-48204N.
    IntActiP0A881. 3 interactions.
    STRINGi511145.b4393.

    Structurei

    Secondary structure

    1
    108
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 3123
    Helixi35 – 428
    Helixi45 – 6319
    Helixi68 – 758
    Helixi79 – 9113
    Helixi94 – 10411
    Turni105 – 1073

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CO0NMR-A/B2-108[»]
    1JHGX-ray1.30A8-108[»]
    1MI7X-ray2.50R2-108[»]
    1RCSNMR-A/B4-107[»]
    1TROX-ray1.90A/C/E/G1-108[»]
    1TRRX-ray2.40A/B/D/E/G/H/J/K2-108[»]
    1WRPX-ray2.20R2-108[»]
    1WRSNMR-R/S4-108[»]
    1WRTNMR-R/S4-108[»]
    1ZT9X-ray2.00A/B/D/E2-108[»]
    2OZ9X-ray1.65R2-108[»]
    3SSWX-ray1.67N/R2-108[»]
    3SSXX-ray1.58N/R2-108[»]
    3WRPX-ray1.80A1-108[»]
    ProteinModelPortaliP0A881.
    SMRiP0A881. Positions 5-108.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A881.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the TrpR family.Curated

    Phylogenomic databases

    eggNOGiCOG2973.
    HOGENOMiHOG000288846.
    KOiK03720.
    OMAiELMRGEM.
    OrthoDBiEOG65TRW3.

    Family and domain databases

    Gene3Di1.10.1270.10. 1 hit.
    HAMAPiMF_00475. Trp_repressor.
    InterProiIPR000831. Trp_repress.
    IPR013335. Trp_repress_bac.
    IPR010921. Trp_repressor/repl_initiator.
    [Graphical view]
    PfamiPF01371. Trp_repressor. 1 hit.
    [Graphical view]
    PIRSFiPIRSF003196. Trp_repressor. 1 hit.
    ProDomiPD012582. Trp_repress_bac. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF48295. SSF48295. 1 hit.
    TIGRFAMsiTIGR01321. TrpR. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0A881-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAQQSPYSAA MAEQRHQEWL RFVDLLKNAY QNDLHLPLLN LMLTPDEREA    50
    LGTRVRIVEE LLRGEMSQRE LKNELGAGIA TITRGSNSLK AAPVELRQWL 100
    EEVLLKSD 108
    Length:108
    Mass (Da):12,355
    Last modified:January 23, 2007 - v2
    Checksum:iFDFF8A60EC4FE7BE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti26 – 261L → V in AAA72134. (PubMed:7841459)Curated
    Sequence conflicti56 – 561R → A in AAA72134. (PubMed:7841459)Curated
    Sequence conflicti100 – 1001L → M in AAA72134. (PubMed:7841459)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01715 Genomic DNA. Translation: AAA72140.1.
    L13768 Genomic DNA. Translation: AAA72134.1.
    U14003 Genomic DNA. Translation: AAA97289.1.
    U00096 Genomic DNA. Translation: AAC77346.1.
    AP009048 Genomic DNA. Translation: BAE78382.1.
    M69185 Genomic DNA. No translation available.
    PIRiA03568. RPECW.
    RefSeqiNP_418810.1. NC_000913.3.
    YP_492523.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC77346; AAC77346; b4393.
    BAE78382; BAE78382; BAE78382.
    GeneIDi12931807.
    948917.
    KEGGiecj:Y75_p4277.
    eco:b4393.
    PATRICi32124404. VBIEscCol129921_4542.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01715 Genomic DNA. Translation: AAA72140.1 .
    L13768 Genomic DNA. Translation: AAA72134.1 .
    U14003 Genomic DNA. Translation: AAA97289.1 .
    U00096 Genomic DNA. Translation: AAC77346.1 .
    AP009048 Genomic DNA. Translation: BAE78382.1 .
    M69185 Genomic DNA. No translation available.
    PIRi A03568. RPECW.
    RefSeqi NP_418810.1. NC_000913.3.
    YP_492523.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CO0 NMR - A/B 2-108 [» ]
    1JHG X-ray 1.30 A 8-108 [» ]
    1MI7 X-ray 2.50 R 2-108 [» ]
    1RCS NMR - A/B 4-107 [» ]
    1TRO X-ray 1.90 A/C/E/G 1-108 [» ]
    1TRR X-ray 2.40 A/B/D/E/G/H/J/K 2-108 [» ]
    1WRP X-ray 2.20 R 2-108 [» ]
    1WRS NMR - R/S 4-108 [» ]
    1WRT NMR - R/S 4-108 [» ]
    1ZT9 X-ray 2.00 A/B/D/E 2-108 [» ]
    2OZ9 X-ray 1.65 R 2-108 [» ]
    3SSW X-ray 1.67 N/R 2-108 [» ]
    3SSX X-ray 1.58 N/R 2-108 [» ]
    3WRP X-ray 1.80 A 1-108 [» ]
    ProteinModelPortali P0A881.
    SMRi P0A881. Positions 5-108.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-48204N.
    IntActi P0A881. 3 interactions.
    STRINGi 511145.b4393.

    Proteomic databases

    PaxDbi P0A881.
    PRIDEi P0A881.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC77346 ; AAC77346 ; b4393 .
    BAE78382 ; BAE78382 ; BAE78382 .
    GeneIDi 12931807.
    948917.
    KEGGi ecj:Y75_p4277.
    eco:b4393.
    PATRICi 32124404. VBIEscCol129921_4542.

    Organism-specific databases

    EchoBASEi EB1022.
    EcoGenei EG11029. trpR.

    Phylogenomic databases

    eggNOGi COG2973.
    HOGENOMi HOG000288846.
    KOi K03720.
    OMAi ELMRGEM.
    OrthoDBi EOG65TRW3.

    Enzyme and pathway databases

    BioCyci EcoCyc:PD00423.
    ECOL316407:JW4356-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A881.
    PROi P0A881.

    Gene expression databases

    Genevestigatori P0A881.

    Family and domain databases

    Gene3Di 1.10.1270.10. 1 hit.
    HAMAPi MF_00475. Trp_repressor.
    InterProi IPR000831. Trp_repress.
    IPR013335. Trp_repress_bac.
    IPR010921. Trp_repressor/repl_initiator.
    [Graphical view ]
    Pfami PF01371. Trp_repressor. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF003196. Trp_repressor. 1 hit.
    ProDomi PD012582. Trp_repress_bac. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF48295. SSF48295. 1 hit.
    TIGRFAMsi TIGR01321. TrpR. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence and expression of Escherichia coli trpR, the structural gene for the trp aporepressor."
      Gunsalus R.P., Yanofsky C.
      Proc. Natl. Acad. Sci. U.S.A. 77:7117-7121(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "DNA sequence of the E. coli trpR gene and prediction of the amino acid sequence of Trp repressor."
      Singleton C.K., Roeder W.D., Bogosian G., Somerville R.L., Weith H.L.
      Nucleic Acids Res. 8:1551-1560(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Bogosian G.
      Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION.
    4. "Nucleotide sequence of the Salmonella typhimurium trpR gene."
      Skrypka I., Somerville R.L.
      DNA Seq. 4:355-360(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
      Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
      Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    7. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    8. "Murein-metabolizing enzymes from Escherichia coli: sequence analysis and controlled overexpression of the slt gene, which encodes the soluble lytic transglycosylase."
      Engel H., Kazemier B., Keck W.
      J. Bacteriol. 173:6773-6782(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    9. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    10. "The crystal structure of trp aporepressor at 1.8 A shows how binding tryptophan enhances DNA affinity."
      Zhang R.-G., Joachimiak A., Lawson C.L., Schevitz R.W., Otwinowski Z., Sigler P.B.
      Nature 327:591-597(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    11. "The structure of trp pseudorepressor at 1.65A shows why indole propionate acts as a trp 'inducer'."
      Lawson C.L., Sigler P.B.
      Nature 333:869-871(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
    12. "Sequence-specific 1H NMR assignments and secondary structure in solution of Escherichia coli trp repressor."
      Arrowsmith C.H., Pachter R., Altman R.B., Iyer S.B., Jardetzky O.
      Biochemistry 29:6332-6341(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    13. "The solution structures of Escherichia coli trp repressor and trp aporepressor at an intermediate resolution."
      Arrowsmith C.H., Pachter R., Altman R.B., Jardetzky O.
      Eur. J. Biochem. 202:53-66(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    14. "Sequence-specific NMR assignments of the trp repressor from Escherichia coli using three-dimensional 15N/1H heteronuclear techniques."
      Borden K.L.B., Bauer C.J., Frenkiel T.A., Beckmann P., Lane A.N.
      Eur. J. Biochem. 204:137-146(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    15. "Refined solution structures of the Escherichia coli trp holo- and aporepressor."
      Zhao D., Arrowsmith C.H., Jia X., Jardetzky O.
      J. Mol. Biol. 229:735-746(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    16. "The solution structures of the trp repressor-operator DNA complex."
      Zhang H., Zhao D., Revington M., Lee W., Jia X., Arrowsmith C.H., Jardetzky O.
      J. Mol. Biol. 238:592-614(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    17. "The stereochemistry and biochemistry of the trp repressor-operator complex."
      Luisi B.F., Sigler P.B.
      Biochim. Biophys. Acta 1048:113-126(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.

    Entry informationi

    Entry nameiTRPR_ECOLI
    AccessioniPrimary (citable) accession number: P0A881
    Secondary accession number(s): P03032, Q2M5S4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 89 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    PubMed:7841459 sequence was originally thought to originate from S.typhimurium, but seems to come from an unknown E.coli strain.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3