Escherichia coli K-12 substr. MG1655 Protein: TorS sensory histidine kinase
Inferred from experiment

Gene: torS Accession Numbers: G6514 (EcoCyc), b0993, ECK0984

Synonyms: yccI

Regulation Summary Diagram

Regulation summary diagram for torS

Subunit composition of TorS sensory histidine kinase = [TorS]2
         TorS monomer = TorS

Alternative forms of TorS monomer:
TorS sensory histidine kinase - his850 phosphorylated (summary available)
TorS sensory histidine kinase - asp723 phosphorylated (summary available)
TorS sensory histidine kinase - his443 phosphorylated (summary available)

TorS is the sensor partner of the periplasmic TorT protein and the TorR response regulator, responding to changes in the concentration of TMAO. TorS consists of an N-terminal detector region followed by a transmitter domain with a histidine phosphorylation site and an ATP binding motif, a receiver domain with an aspartate phosphorylation site, and a C-terminal alternative transmitter domain with a phosphorylation site. All three phosphorylation sites are essential for function. The C-terminal alternative transmitter domain contains the phosphodonor site for TorR [Jourlin97]. TorR is thus transphosphorylated by a four-step phosphorelay, beginning with autophosphorylation of TorS at His443, transfer of the phosphate group to Asp723 and finally His850, which then transfers the phosphate to TorR.

TorS may also be able to dephosphorylate TorR via a reverse phosphorelay when the TMAO inducer is removed [Ansaldi01]. The C-terminal domain of the immature form of TorC, a c-type cytochrome, can interact with the periplasmic detector region of TorS and downregulate its own expression, presumably via dephosphorylation of TorR [Ansaldi99, Gon01].

Certain mutations in torS cause TMAO-independent expression of the tor operon. One allele appears to affect the TMAO binding site, while two alleles localize to the linker region between the sensor and transmitter domains. A torS null mutation abolishes tor operon expression under all tested growth conditions. Overexpression of TorR bypasses the requirement for TorS, and TorT is dispensable in a torS constitutive mutant [Jourlin96a]. Complementation between torS mutants defective at different sites suggests that TorS forms multimers [Jourlin97].

Locations: inner membrane

Map Position: [1,053,434 <- 1,056,178] (22.7 centisomes, 82°)
Length: 2745 bp / 914 aa

Molecular Weight of Polypeptide: 101.02 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0003354, DIP:DIP-11017N, EchoBASE:EB2501, EcoGene:EG12617, EcoliWiki:b0993, ModBase:P39453, OU-Microarray:b0993, PortEco:torS, PR:PRO_000024090, Pride:P39453, Protein Model Portal:P39453, RegulonDB:G6514, SMR:P39453, String:511145.b0993, UniProt:P39453

Relationship Links: InterPro:IN-FAMILY:IPR001789, InterPro:IN-FAMILY:IPR003594, InterPro:IN-FAMILY:IPR003660, InterPro:IN-FAMILY:IPR003661, InterPro:IN-FAMILY:IPR004358, InterPro:IN-FAMILY:IPR005467, InterPro:IN-FAMILY:IPR008207, InterPro:IN-FAMILY:IPR009082, InterPro:IN-FAMILY:IPR011006, InterPro:IN-FAMILY:IPR014302, PDB:Structure:3I9W, Pfam:IN-FAMILY:PF00072, Pfam:IN-FAMILY:PF00512, Pfam:IN-FAMILY:PF00672, Pfam:IN-FAMILY:PF01627, Pfam:IN-FAMILY:PF02518, Prints:IN-FAMILY:PR00344, Prosite:IN-FAMILY:PS50109, Prosite:IN-FAMILY:PS50110, Prosite:IN-FAMILY:PS50885, Prosite:IN-FAMILY:PS50894, Smart:IN-FAMILY:SM00073, Smart:IN-FAMILY:SM00304, Smart:IN-FAMILY:SM00387, Smart:IN-FAMILY:SM00388, Smart:IN-FAMILY:SM00448

In Paralogous Gene Group: 121 (40 members), 122 (29 members)

Reactions known to consume the compound:

TorSR Two-Component Signal Transduction System, TMAO dependent :
ATP + TorS sensory histidine kinase → ADP + TorS sensory histidine kinase - his443 phosphorylated

Reactions known to produce the compound:

TorSR Two-Component Signal Transduction System, TMAO dependent :
TorS sensory histidine kinase - his850 phosphorylated + TorR → TorS sensory histidine kinase + TorR-Pasp

Gene-Reaction Schematic

Gene-Reaction Schematic

GO Terms:
Biological Process:
Inferred from experimentInferred by computational analysisGO:0000160 - phosphorelay signal transduction system [UniProtGOA11a, GOA01a, Jourlin97]
Inferred from experimentGO:0006470 - protein dephosphorylation [Ansaldi01]
Inferred from experimentGO:0009061 - anaerobic respiration [Jourlin96a]
Inferred from experimentInferred by computational analysisGO:0023014 - signal transduction by protein phosphorylation [GOA01a, Jourlin96a]
Inferred from experimentGO:0046777 - protein autophosphorylation [Jourlin97]
Inferred from experimentGO:0071310 - cellular response to organic substance [Jourlin96a]
Inferred by computational analysisGO:0007165 - signal transduction [GOA01a]
Inferred by computational analysisGO:0016310 - phosphorylation [UniProtGOA11a, GOA01a]
Inferred by computational analysisGO:0018106 - peptidyl-histidine phosphorylation [GOA01, GOA01a]
Molecular Function:
Inferred from experimentInferred by computational analysisGO:0000155 - phosphorelay sensor kinase activity [GOA01a, Jourlin96a]
Inferred from experimentGO:0004721 - phosphoprotein phosphatase activity [Ansaldi01]
Inferred from experimentGO:0005515 - protein binding [Gon01]
Inferred from experimentInferred by computational analysisGO:0016772 - transferase activity, transferring phosphorus-containing groups [GOA01a, Jourlin97]
Inferred from experimentGO:0016868 - intramolecular transferase activity, phosphotransferases [Jourlin97]
Inferred from experimentGO:0042803 - protein homodimerization activity [Jourlin97]
Inferred by computational analysisGO:0000166 - nucleotide binding [UniProtGOA11a]
Inferred by computational analysisGO:0004673 - protein histidine kinase activity [GOA01, GOA01a]
Inferred by computational analysisGO:0004871 - signal transducer activity [GOA01a]
Inferred by computational analysisGO:0005524 - ATP binding [UniProtGOA11a]
Inferred by computational analysisGO:0016301 - kinase activity [UniProtGOA11a]
Inferred by computational analysisGO:0016740 - transferase activity [UniProtGOA11a]
Cellular Component:
Inferred from experimentInferred by computational analysisGO:0005622 - intracellular [UniProtGOA11a, GOA01a, Jourlin97]
Inferred from experimentInferred by computational analysisGO:0005886 - plasma membrane [UniProtGOA11, UniProtGOA11a, DiazMejia09, Daley05, Jourlin96a]
Inferred by computational analysisGO:0005887 - integral component of plasma membrane [Jourlin96a]
Inferred by computational analysisGO:0016020 - membrane [UniProtGOA11a]
Inferred by computational analysisGO:0016021 - integral component of membrane [UniProtGOA11a, GOA01a]

MultiFun Terms: cell structuremembrane
information transferprotein relatedposttranslational modification
metabolismenergy metabolism, carbonanaerobic respiration
regulationtype of regulationposttranscriptionalcovalent modification, demodification, maturation
regulationtype of regulationtranscriptional levelcomplex regulationtwo component regulatory systems (external signal)

Essentiality data for torS knockouts:

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enrichedYes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB LennoxYes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerolYes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucoseYes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Sequence Features

Protein sequence of TorS monomer with features indicated

Feature Class Location Citations Comment State
Transmembrane-Region 9 -> 29
Inferred by computational analysis[UniProt15]
UniProt: Helical.
Extrinsic-Sequence-Variant 295 -> 297
Author statement[UniProt15]
UniProt: In torS726; constitutively active..
Transmembrane-Region 333 -> 353
Inferred by computational analysis[UniProt15]
UniProt: Helical.
Conserved-Region 354 -> 407
Inferred by computational analysis[UniProt15]
UniProt: HAMP.
Extrinsic-Sequence-Variant 408
Author statement[UniProt15]
UniProt: In torS729; partial activation..
Extrinsic-Sequence-Variant 414
Author statement[UniProt15]
UniProt: In torS13; partial activation..
Conserved-Region 450 -> 664
Inferred by computational analysis[UniProt15]
UniProt: Histidine kinase.
Mutagenesis-Variant 453
Inferred from experiment[Jourlin97]
UniProt: Loss of activity.
Phosphorylation-Modification 453
Inferred by computational analysis[UniProt13]
UniProt: Phosphohistidine; by autocatalysis; Non-Experimental Qualifier: probable.
Conserved-Region 683 -> 798
Inferred by computational analysis[UniProt15]
UniProt: Response regulatory.
Mutagenesis-Variant 733
Inferred from experiment[Jourlin97]
D → A or E: Loss of activity.
4-aspartylphosphate-Modification 733
Inferred by computational analysis[UniProt11]
UniProt: 4-aspartylphosphate; Non-Experimental Qualifier: probable.
Sequence-Conflict 771 -> 772
Inferred by curator[Jourlin96a, UniProt15]
UniProt: (in Ref. 1; CAA63920).
Conserved-Region 821 -> 914
Inferred by computational analysis[UniProt15]
UniProt: HPt.
Mutagenesis-Variant 860
Inferred from experiment[Jourlin97]
UniProt: Decrease in activity.
Phosphorylation-Modification 860
Inferred by computational analysis[UniProt13]
UniProt: Phosphohistidine; Non-Experimental Qualifier: probable.

Sequence Pfam Features

Protein sequence of TorS monomer with features indicated

Feature Class Location Citations Comment
Pfam PF00672 334 -> 404
Inferred by computational analysis[Finn14]
HAMP : HAMP domain
Pfam PF00512 443 -> 508
Inferred by computational analysis[Finn14]
HisKA : His Kinase A (phospho-acceptor) domain [More...]
Pfam PF02518 557 -> 662
Inferred by computational analysis[Finn14]
HATPase_c : Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase [More...]
Pfam PF00072 685 -> 792
Inferred by computational analysis[Finn14]
Response_reg : Response regulator receiver domain [More...]
Pfam PF01627 827 -> 905
Inferred by computational analysis[Finn14]
Hpt : Hpt domain [More...]

Gene Local Context (not to scale -- see Genome Browser for correct scale)

Transcription Unit

Transcription-unit diagram


Peter D. Karp on Wed Jan 18, 2006:
Gene right-end position adjusted based on analysis performed in the 2005 E. coli annotation update [Riley06].
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


Ansaldi01: Ansaldi M, Jourlin-Castelli C, Lepelletier M, Theraulaz L, Mejean V (2001). "Rapid dephosphorylation of the TorR response regulator by the TorS unorthodox sensor in Escherichia coli." J Bacteriol 2001;183(8);2691-5. PMID: 11274133

Ansaldi99: Ansaldi M, Bordi C, Lepelletier M, Mejean V (1999). "TorC apocytochrome negatively autoregulates the trimethylamine N-oxide (TMAO) reductase operon in Escherichia coli." Mol Microbiol 33(2);284-95. PMID: 10411745

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Daley05: Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308(5726);1321-3. PMID: 15919996

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Finn14: Finn RD, Bateman A, Clements J, Coggill P, Eberhardt RY, Eddy SR, Heger A, Hetherington K, Holm L, Mistry J, Sonnhammer EL, Tate J, Punta M (2014). "Pfam: the protein families database." Nucleic Acids Res 42(Database issue);D222-30. PMID: 24288371

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Gon01: Gon S, Jourlin-Castelli C, Theraulaz L, Mejean V (2001). "An unsuspected autoregulatory pathway involving apocytochrome TorC and sensor TorS in Escherichia coli." Proc Natl Acad Sci U S A 98(20);11615-20. PMID: 11562502

Jourlin96a: Jourlin C, Bengrine A, Chippaux M, Mejean V (1996). "An unorthodox sensor protein (TorS) mediates the induction of the tor structural genes in response to trimethylamine N-oxide in Escherichia coli." Mol Microbiol 1996;20(6);1297-306. PMID: 8809780

Jourlin97: Jourlin C, Ansaldi M, Mejean V (1997). "Transphosphorylation of the TorR response regulator requires the three phosphorylation sites of the TorS unorthodox sensor in Escherichia coli." J Mol Biol 1997;267(4);770-7. PMID: 9135110

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Riley06: Riley M, Abe T, Arnaud MB, Berlyn MK, Blattner FR, Chaudhuri RR, Glasner JD, Horiuchi T, Keseler IM, Kosuge T, Mori H, Perna NT, Plunkett G, Rudd KE, Serres MH, Thomas GH, Thomson NR, Wishart D, Wanner BL (2006). "Escherichia coli K-12: a cooperatively developed annotation snapshot--2005." Nucleic Acids Res 34(1);1-9. PMID: 16397293

UniProt11: UniProt Consortium (2011). "UniProt version 2011-11 released on 2011-11-22 00:00:00." Database.

UniProt13: UniProt Consortium (2013). "UniProt version 2013-08 released on 2013-08-01 00:00:00." Database.

UniProt15: UniProt Consortium (2015). "UniProt version 2015-08 released on 2015-07-22." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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