P38684 (TORR_ECOLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 118.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: TorCAD operon transcriptional regulatory protein TorR | ||||
| Gene names |
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| Organism | Escherichia coli (strain K12) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 83333 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › ![]() |
Protein attributes
| Sequence length | 230 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transcription Transcription regulation Two-component regulatory system |
| Cellular component | Cytoplasm |
| Ligand | DNA-binding |
| Molecular function | Activator |
| PTM | Phosphoprotein |
| Technical term | 3D-structure Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | regulation of transcription, DNA-dependent Inferred from direct assay Ref.1. Source: EcoCyc transcription, DNA-dependentInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | DNA binding Inferred from electronic annotation. Source: UniProtKB-KW phosphorelay response regulator activityInferred from direct assay Ref.1. Source: EcoCyc |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 230 | 230 | TorCAD operon transcriptional regulatory protein TorR | PRO_0000081255 | ||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||
| Domain | 1 – 117 | 117 | Response regulatory | |||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||
| Modified residue | 53 | 1 | 4-aspartylphosphate Probable | |||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||
| Mutagenesis | 53 | 1 | D → A: Loss of phosphorylation. Ref.7 | |||||||||||||||||||||||||||
| Sequence conflict | 134 | 1 | C → L in CAA63922. Ref.1 | |||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||
| Beta strand | 4 – 8 | 5 | ||||||||||||||||||||||||||||
| Helix | 12 – 24 | 13 | ||||||||||||||||||||||||||||
| Beta strand | 28 – 34 | 7 | ||||||||||||||||||||||||||||
| Helix | 35 – 44 | 10 | ||||||||||||||||||||||||||||
| Beta strand | 48 – 54 | 7 | ||||||||||||||||||||||||||||
| Beta strand | 57 – 59 | 3 | ||||||||||||||||||||||||||||
| Helix | 61 – 69 | 9 | ||||||||||||||||||||||||||||
| Beta strand | 75 – 82 | 8 | ||||||||||||||||||||||||||||
| Helix | 85 – 94 | 10 | ||||||||||||||||||||||||||||
| Beta strand | 97 – 103 | 7 | ||||||||||||||||||||||||||||
| Helix | 106 – 120 | 15 | ||||||||||||||||||||||||||||
Sequences
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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. 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. | ||||||||||||
| PIR | A64841. | ||||||||||||
| RefSeq | NP_415515.1. NC_000913.2. YP_489268.1. NC_007779.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P38684. | ||||||||||||
| SMR | P38684. Positions 2-225. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| DIP | DIP-11016N. | ||||||||||||
| IntAct | P38684. 3 interactions. | ||||||||||||
| MINT | MINT-1283676. | ||||||||||||
| STRING | 511145.b0995. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblBacteria | AAC74080; AAC74080; b0995. BAA36137; BAA36137; BAA36137. | ||||||||||||
| GeneID | 12932494. 946182. | ||||||||||||
| KEGG | ecj:Y75_p0968. eco:b0995. | ||||||||||||
| PATRIC | 32117215. VBIEscCol129921_1031. | ||||||||||||
Organism-specific databases | |||||||||||||
| EchoBASE | EB2499. | ||||||||||||
| EcoGene | EG12615. torR. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG0745. | ||||||||||||
| HOGENOM | HOG000034819. | ||||||||||||
| KO | K07772. | ||||||||||||
| OMA | YCYRFAG. | ||||||||||||
| ProtClustDB | PRK10766. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | EcoCyc:TORR-MONOMER. ECOL316407:JW0980-MONOMER. | ||||||||||||
Gene expression databases | |||||||||||||
| Genevestigator | P38684. | ||||||||||||
Family and domain databases | |||||||||||||
| Gene3D | 1.10.10.10. 1 hit. | ||||||||||||
| InterPro | IPR011006. CheY-like_superfamily. IPR001867. Sig_transdc_resp-reg_C. IPR001789. Sig_transdc_resp-reg_receiver. IPR011991. WHTH_DNA-bd_dom. [Graphical view] | ||||||||||||
| Pfam | PF00072. Response_reg. 1 hit. PF00486. Trans_reg_C. 1 hit. [Graphical view] | ||||||||||||
| SMART | SM00448. REC. 1 hit. SM00862. Trans_reg_C. 1 hit. [Graphical view] | ||||||||||||
| SUPFAM | SSF52172. CheY_like. 1 hit. | ||||||||||||
| PROSITE | PS50110. RESPONSE_REGULATORY. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | P38684. | ||||||||||||
Entry information
| Entry name | TORR_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P38684 Secondary accession number(s): P77344 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic 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 |

Clusters with
