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P38684 (TORR_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
TorCAD operon transcriptional regulatory protein TorR
Gene names
Name:torR
Ordered Locus Names:b0995, JW0980
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length230 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Member of the two-component regulatory system TorS/TorR involved in the anaerobic utilization of trimethylamine-N-oxide (TMAO). Phosphorylated TorR activates the transcription of the torCAD operon by binding to four decameric boxes located in the torCAD promoter. Box1, 2 and 4 contain the DNA sequence 5'-CTGTTCATAT-3' and box3 contains the DNA sequence 5'-CCGTTCATCC-3'. Phosphorylated as well as unphosphorylated TorR negatively regulates its own expression by binding to box1 and 2.

Subunit structure

Interacts with TorI. TorI binds to the effector domain of TorR. This interaction, which does not interfere with TorR DNA binding activity, probably prevents the recruitment of RNA polymerase to the torCAD promoter. Ref.9

Subcellular location

Cytoplasm Probable.

Post-translational modification

Phosphorylated and dephosphorylated by TorS.

Sequence similarities

Contains 1 response regulatory domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 230230TorCAD operon transcriptional regulatory protein TorR
PRO_0000081255

Regions

Domain1 – 117117Response regulatory

Amino acid modifications

Modified residue5314-aspartylphosphate Probable

Experimental info

Mutagenesis531D → A: Loss of phosphorylation. Ref.7
Sequence conflict1341C → L in CAA63922. Ref.1

Secondary structure

...................... 230
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P38684 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: D1936404503FBA09

FASTA23026,233
        10         20         30         40         50         60 
MPHHIVIVED EPVTQARLQS YFTQEGYTVS VTASGAGLRE IMQNQSVDLI LLDINLPDEN 

        70         80         90        100        110        120 
GLMLTRALRE RSTVGIILVT GRSDRIDRIV GLEMGADDYV TKPLELRELV VRVKNLLWRI 

       130        140        150        160        170        180 
DLARQAQPHT QDNCYRFAGY CLNVSRHTLE RDGEPIKLTR AEYEMLVAFV TNPGEILSRE 

       190        200        210        220        230 
RLLRMLSARR VENPDLRTVD VLIRRLRHKL SADLLVTQHG EGYFLAADVC 

« Hide

References

« Hide 'large scale' references
[1]"The torR gene of Escherichia coli encodes a response regulator protein involved in the expression of the trimethylamine N-oxide reductase genes."
Simon G., Mejean V., Jourlin C., Chippaux M., Pascal M.-C.
J. Bacteriol. 176:5601-5606(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-7.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[2]Erratum
Simon G., Mejean V., Jourlin C., Chippaux M., Pascal M.-C.
J. Bacteriol. 177:275-275(1995) [PubMed] [Europe PMC] [Abstract]
[3]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"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 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"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.
[6]"Binding of the TorR regulator to cis-acting direct repeats activates tor operon expression."
Simon G., Jourlin C., Ansaldi M., Pascal M.-C., Chippaux M., Mejean V.
Mol. Microbiol. 17:971-980(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[7]"Transphosphorylation of the TorR response regulator requires the three phosphorylation sites of the TorS unorthodox sensor in Escherichia coli."
Jourlin C., Ansaldi M., Mejean V.
J. Mol. Biol. 267:770-777(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASP-53.
[8]"The TorR high-affinity binding site plays a key role in both torR autoregulation and torCAD operon expression in Escherichia coli."
Ansaldi M., Simon G., Lepelletier M., Mejean V.
J. Bacteriol. 182:961-966(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[9]"TorI, a response regulator inhibitor of phage origin in Escherichia coli."
Ansaldi M., Theraulaz L., Mejean V.
Proc. Natl. Acad. Sci. U.S.A. 101:9423-9428(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TORI.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X94231 Genomic DNA. Translation: CAA63922.1.
U00096 Genomic DNA. Translation: AAC74080.1.
AP009048 Genomic DNA. Translation: BAA36137.1.
PIRA64841.
RefSeqNP_415515.1. NC_000913.2.
YP_489268.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZGZX-ray1.80A/B/C/D1-121[»]
ProteinModelPortalP38684.
SMRP38684. Positions 2-225.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-11016N.
IntActP38684. 3 interactions.
MINTMINT-1283676.
STRING511145.b0995.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74080; AAC74080; b0995.
BAA36137; BAA36137; BAA36137.
GeneID12932494.
946182.
KEGGecj:Y75_p0968.
eco:b0995.
PATRIC32117215. VBIEscCol129921_1031.

Organism-specific databases

EchoBASEEB2499.
EcoGeneEG12615. torR.

Phylogenomic databases

eggNOGCOG0745.
HOGENOMHOG000034819.
KOK07772.
OMAYCYRFAG.
ProtClustDBPRK10766.

Enzyme and pathway databases

BioCycEcoCyc:TORR-MONOMER.
ECOL316407:JW0980-MONOMER.

Gene expression databases

GenevestigatorP38684.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR011006. CheY-like_superfamily.
IPR001867. Sig_transdc_resp-reg_C.
IPR001789. Sig_transdc_resp-reg_receiver.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00072. Response_reg. 1 hit.
PF00486. Trans_reg_C. 1 hit.
[Graphical view]
SMARTSM00448. REC. 1 hit.
SM00862. Trans_reg_C. 1 hit.
[Graphical view]
SUPFAMSSF52172. CheY_like. 1 hit.
PROSITEPS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP38684.

Entry information

Entry nameTORR_ECOLI
AccessionPrimary (citable) accession number: P38684
Secondary accession number(s): P77344
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 1, 1997
Last modified: May 1, 2013
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families