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P0A881 (TRPR_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Trp operon repressor
Gene names
Name:trpR
Synonyms:rtrY
Ordered Locus Names:b4393, JW4356
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length108 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_00475

Subunit structure

Homodimer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00475.

Sequence similarities

Belongs to the TrpR family.

Caution

Ref.4 sequence was originally thought to originate from S.typhimurium, but seems to come from an unknown E.coli strain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed HAMAP-Rule MF_00475
Chain2 – 108107Trp operon repressor HAMAP-Rule MF_00475
PRO_0000196494

Regions

DNA binding68 – 9124 HAMAP-Rule MF_00475

Experimental info

Sequence conflict261L → V in AAA72134. Ref.4
Sequence conflict561R → A in AAA72134. Ref.4
Sequence conflict1001L → M in AAA72134. Ref.4

Secondary structure

.............. 108
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A881 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: FDFF8A60EC4FE7BE

FASTA10812,355
        10         20         30         40         50         60 
MAQQSPYSAA MAEQRHQEWL RFVDLLKNAY QNDLHLPLLN LMLTPDEREA LGTRVRIVEE 

        70         80         90        100 
LLRGEMSQRE LKNELGAGIA TITRGSNSLK AAPVELRQWL EEVLLKSD 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRRPECW. A03568.
RefSeqNP_418810.1. NC_000913.3.
YP_492523.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CO0NMR-A/B2-107[»]
1JHGX-ray1.30A8-107[»]
1MI7X-ray2.50R2-107[»]
1RCSNMR-A/B4-108[»]
1TROX-ray1.90A/C/E/G1-108[»]
1TRRX-ray2.40A/B/D/E/G/H/J/K2-107[»]
1WRPX-ray2.20R2-107[»]
1WRSNMR-R/S4-108[»]
1WRTNMR-R/S4-108[»]
1ZT9X-ray2.00A/B/D/E2-107[»]
2OZ9X-ray1.65R2-108[»]
3SSWX-ray1.67N/R2-108[»]
3SSXX-ray1.58N/R2-108[»]
3WRPX-ray1.80A2-107[»]
ProteinModelPortalP0A881.
SMRP0A881. Positions 5-108.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48204N.
IntActP0A881. 3 interactions.
STRING511145.b4393.

Proteomic databases

PaxDbP0A881.
PRIDEP0A881.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC77346; AAC77346; b4393.
BAE78382; BAE78382; BAE78382.
GeneID12931807.
948917.
KEGGecj:Y75_p4277.
eco:b4393.
PATRIC32124404. VBIEscCol129921_4542.

Organism-specific databases

EchoBASEEB1022.
EcoGeneEG11029. trpR.

Phylogenomic databases

eggNOGCOG2973.
HOGENOMHOG000288846.
KOK03720.
OMAELMRGEM.
OrthoDBEOG65TRW3.
ProtClustDBPRK01381.

Enzyme and pathway databases

BioCycEcoCyc:PD00423.
ECOL316407:JW4356-MONOMER.

Gene expression databases

GenevestigatorP0A881.

Family and domain databases

Gene3D1.10.1270.10. 1 hit.
HAMAPMF_00475. Trp_repressor.
InterProIPR000831. Trp_repress.
IPR013335. Trp_repress_bac.
IPR010921. Trp_repressor/repl_initiator.
[Graphical view]
PfamPF01371. Trp_repressor. 1 hit.
[Graphical view]
PIRSFPIRSF003196. Trp_repressor. 1 hit.
ProDomPD012582. Trp_repress_bac. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF48295. SSF48295. 1 hit.
TIGRFAMsTIGR01321. TrpR. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0A881.
PROP0A881.

Entry information

Entry nameTRPR_ECOLI
AccessionPrimary (citable) accession number: P0A881
Secondary accession number(s): P03032, Q2M5S4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene