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Protein

Trp operon repressor

Gene

trpR

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

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
Complete GO annotation...

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
Complete GO annotation...

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 – 3123Combined sources
Helixi35 – 428Combined sources
Helixi45 – 6319Combined sources
Helixi68 – 758Combined sources
Helixi79 – 9113Combined sources
Helixi94 – 10411Combined sources
Turni105 – 1073Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP0A881.
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

        10         20         30         40         50
MAQQSPYSAA MAEQRHQEWL RFVDLLKNAY QNDLHLPLLN LMLTPDEREA
60 70 80 90 100
LGTRVRIVEE LLRGEMSQRE LKNELGAGIA TITRGSNSLK AAPVELRQWL

EEVLLKSD
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

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

Chemistry

BindingDBiP0A881.

Proteomic databases

PaxDbiP0A881.
PRIDEiP0A881.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EchoBASEiEB1022.
EcoGeneiEG11029. trpR.

Phylogenomic databases

eggNOGiCOG2973.
HOGENOMiHOG000288846.
InParanoidiP0A881.
KOiK03720.
OMAiELMRGEM.
OrthoDBiEOG65TRW3.

Enzyme and pathway databases

BioCyciEcoCyc:PD00423.
ECOL316407:JW4356-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A881.
PROiP0A881.

Gene expression databases

GenevestigatoriP0A881.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: January 7, 2015
This is version 92 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.