Escherichia coli K-12 substr. MG1655 Protein: chemotaxis signaling complex - ribose/galactose/glucose sensing
Inferred from experiment

Synonyms: MCP-III signaling complex

Superclasses: Trg-Un

Subunit composition of chemotaxis signaling complex - ribose/galactose/glucose sensing = [(CheA)2][CheW]2[(Trg)2]3
         CheA(L) histidine kinase = (CheA)2
         methyl accepting chemotaxis protein - ribose/galactose/glucose sensing = (Trg)2 (extended summary available)

Alternative forms of CheA: CheA(L) sensory histidine kinase - phosphorylated (summary available)

Alternative forms of chemotaxis signaling complex - ribose/galactose/glucose sensing:

Chemotaxis in Escherichia coli is accomplished with a modified two-component signal transduction complex which transmits controlling signals to the flagellar motor complex. E.coli has four methyl-accepting chemotaxis protein (MCP)-type receptor complexes which recognize the following ligands: Tsr, serine;Tar, aspartate and maltose;Trg, ribose, galactose and glucose and Tap, dipeptides. Serine and aspartate bind directly to the receptor whereas maltose, ribose, galactose, glucose and dipeptides bind first to a periplasmic binding protein which then docks with its individual membrane receptor [Manson98].

The receptor complexes are ternary structures. The receptor-ligand interaction domain is located in the periplasm. Each receptor serves as the organizational framework for a receptor kinase signaling supermolecular complex formed in conjunction with histidine kinase CheA and other components of the signaling pathway [Falke97]. There are two transmembrane (TM) linker domains (CheW) which couple the methylation-dependent receptor to CheA. The receptors form homodimers with or without ligands [Gegner92]. CheA is a histidine kinase capable of autophosphorylation using ATP as a phosphodonor. The receptor complex dimers form trigonal units which in turn form a two-dimensional hexagonal lattice [Shimizu00] located usually at one pole of the cell. The Tsr and Tar receptors are the most abundant and the Tap, Trg receptors are less prevalent [Bren00].

CheA and CheY comprise a two-component signal transduction system where the signal is transmitted via phosphorylation from CheA to CheY (the response regulator). In several ways CheA/CheY differs from the standard two-component paradigm. Most significantly, CheY does not possess a DNA-binding domain and it doesn't act as a transcription factor. In the absence of activator ligand, CheA autophosphorylation is stimulated thus increasing the phosphotransfer from CheA to CheY, the messenger protein. CheY-P has a lower affinity for CheA than CheY, resulting in the dissociation of CheY-P from CheA. CheY-P has a higher affinity than CheY for the flagellar motor protein, FliM, a component of the motor supramolecular complex [Welch93]. Binding of CheY to FliM increases the probability of flagellar rotation in the CW direction [Barak92a]. CCW rotation of the motor induces the flagellar filaments to coalesce into a bundle which propels the cell forward in a fairly straight line (run). CW rotation disrupts the bundle and causes the cell to tumble. The cell typically travels in a three-dimensional walk consisting of runs interspersed with random chaotic tumbling. CheZ is a cytosolic phosphatase which prevents overaccumulation of CheY-P by accelerating the decay of its aspartyl-phosphate residue [Hess87].

CheY-P is thus maintained during steady-state conditions at a level that generates the random walk [Manson98]. When an attractant molecule binds to the receptor, a conformational change is induced [Yeh93] which propagates across the membrane and results in a suppression of CheA autophosphorylation. Levels of CheY-P decrease and the cells tumble less frequently, causing an increase in their run lengths as they enter areas of higher attractant concentrations. The adaptation response is necessary, though, for the cells to respond properly to continually increasing attractant concentration. Adaptive methylation is carried out by two enzymes: the methyltransferase CheR and the methylesterase CheB [Toews79]. CheR is a constitutive enzyme which, through the use of S-adenosylmethionine, methylates glutamate residues in the cytoplasmic domains of the MCPs. CheB is a target for phosphotransfer from CheA, and the activated CheB-P functions as a methyl esterase which removes methyl groups from the MCPs, reducing their kinase activity. Under steady-state conditions, the addition of methyl groups by CheR is balanced by the methyl group removal by CheB-P and an intermediate level of receptor methylation is maintained, resulting in run-tumble behavior of the cell. When an attractant binds to a receptor and inhibits CheA activity, the levels of CheB-P drop. The decrease is slower than that for CheY-P though, since CheB-P is not a phosphate donor to CheZ. The rising level of methyl esters eventually stimulate histidine kinase activity and therefore counteract the effect of attractant binding to the receptor. This resets the receptor signal to its basal level [Falke97].

The components of the chemotaxis sensory system are arranged at one of the cell poles in tight clusters containing thousands of copies of each protein [Sourjik00]. Binding of an attractant results in an increase in the probability that CheA is inactive (unphosphorylated) and methylation of CheA on four specific glutamate residues increases the probability that that it is active (phosphorylated) [Borkovich92]. Lower levels of methylation reduce the activity of CheA but increase the affinity of the receptor for its attractant ligand [Li00c].

Reviews: [Stock00a, Hazelbauer08, Sourjik04, Sourjik10]

Citations: [Neumann10]

Gene-Reaction Schematic

Expand/Contract the Schematic connections:

Gene-Reaction Schematic

Subunit of chemotaxis signaling complex - ribose/galactose/glucose sensing: CheA(L) histidine kinase

Synonyms: chemotaxis kinase-phosphotransferase CheA(L)

Gene: cheA Accession Numbers: EG10146 (EcoCyc), b1888, ECK1889

Locations: inner membrane, cytosol

Subunit composition of CheA(L) histidine kinase = [CheA]2

Map Position: [1,973,360 <- 1,975,324] (42.51 centisomes, 153°)
Length: 1965 bp / 654 aa

Molecular Weight of Polypeptide: 71.382 kD (from nucleotide sequence)

pI: 4.96

GO Terms:
Biological Process:
Inferred from experimentInferred by computational analysisGO:0000160 - phosphorelay signal transduction system [UniProtGOA11a, GOA01a, Igo89]
Inferred from experimentInferred by computational analysisGO:0016310 - phosphorylation [UniProtGOA11a, GOA01a, Igo89]
Inferred from experimentGO:0031400 - negative regulation of protein modification process [Barak04]
Inferred from experimentGO:0046777 - protein autophosphorylation [Igo89]
Inferred by computational analysisGO:0006935 - chemotaxis [UniProtGOA11a, GOA01a]
Inferred by computational analysisGO:0007165 - signal transduction [GOA01a]
Inferred by computational analysisGO:0018106 - peptidyl-histidine phosphorylation [GOA01, GOA01a]
Inferred by computational analysisGO:0023014 - signal transduction by protein phosphorylation [GOA01a]
Molecular Function:
Inferred from experimentGO:0005515 - protein binding [Thakor11, Rajagopala09, OConnor09, Hao09]
Inferred by computational analysisGO:0000155 - phosphorelay sensor kinase activity [GOA01a]
Inferred by computational analysisGO:0000166 - nucleotide binding [UniProtGOA11a]
Inferred by computational analysisGO:0004673 - protein histidine kinase activity [GOA01a, GOA01]
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]
Inferred by computational analysisGO:0016772 - transferase activity, transferring phosphorus-containing groups [GOA01a]
Cellular Component:
Inferred from experimentGO:0005829 - cytosol [Ridgway77]
Inferred from experimentGO:0005886 - plasma membrane [Ridgway77]
Inferred by computational analysisGO:0005737 - cytoplasm [UniProtGOA11, UniProtGOA11a, GOA01a]

MultiFun Terms: cell processesmotility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
information transferprotein relatedposttranslational modification

Unification Links: EcoliWiki:b1888, ModBase:P07363, Swiss-Model:P07363

Relationship Links: Pfam:IN-FAMILY:PF01584, Pfam:IN-FAMILY:PF01627, Pfam:IN-FAMILY:PF02518, Pfam:IN-FAMILY:PF02895, Pfam:IN-FAMILY:PF09078, UniProt:RELATED-TO:P07363

Reactions known to consume the compound:

Aerotactic Two-Component Signal Transduction System , Chemotactic Two-Component Signal Transduction :
CheA + ATP → CheA-P + ADP

Reactions known to produce the compound:

Aerotactic Two-Component Signal Transduction System :
CheY + CheA-P → CheY-Pasp + CheA

Chemotactic Two-Component Signal Transduction :
CheA-P + CheB → CheA + CheB-Pasp
CheY + CheA-P → CheY-Pasp + CheA

The cheA gene is translated in two isoforms. The small form, CheA(S), arises due to a second translational start site 291 bases downstream of the translation start site for the large form, CheA(L) [Hoch95, Neidhardt96].

The "Spliced Nucleotide Sequence" link above refers to the smaller variant, but note that no splicing occurs.
CheA is the histidine kinase component of the chemotaxis two-component signal transduction complex. The chemotaxis system propagates changes in extracellular chemical concentrations to the flagellar switch complex to regulate swimming behavior. CheA and CheY comprise a two-component signal transduction system where the signal generated by the periplasmic receptor occupancy through a protein-protein interaction with the CheA cytoplasmic component is transmitted via phosphorylation from autophosphorylating histidine kinase CheA to CheY (the response regulator) [Welch93]. The receptor complexes ( MCPI, MCPII, MCPIII and MCPIV) are ternary structures consisting of receptors, CheA and the adaptor protein CheW.

Escherichia coli expresses CheA as both a full length molecule as well as a shorter version translated from an alternative start codon known as CheA(short), which contains a catalytic domain but no kinase substrate domain [Kofoid91]. As a result, a heterodimer containing a full-length CheA alongside a CheA(s) exhibits a fivefold higher autophosphorylation rate than the CheA homodimer [Levit96].

CheA autophosphorylates on His48 in the presence of ATP in vitro. The phosphate group on CheA can be transferred to CheB or to CheY in vitro [Hess88, Hess88a]. CheA is a dimer in solution. Two CheW monomers bind per CheA dimer [Gegner91]. CheA autophosphorylation results from transphosphorylation within the dimer [Swanson93a]. In an in vitro reconstituted system, autophosphorylation of purified CheA is stimulated by addition of wild type Tar receptor and CheW protein [Borkovich90, Borkovich89]. CheA contains separate functional domains associated with kinase activity, CheY binding, phosphotransfer activity and receptor binding [Swanson93, Bourret93, Morrison94, Stewart00, Stewart04, Bhatnagar12]. CheA interacts with chemoreceptors in a manner similar to CheW; CheA and CheW bind to the same region of chemoreceptors due to structural similarity between CheW and the regulatory or P5 domain of CheA [Wang12]. Chemotaxis receptors control kinase activity by regulating CheA domain mobility [Briegel13].

Citations: [Zhao06, Levit02, Francis04, Morrison97, Piasta13, Garzon96, Thakor11]

Gene Citations: [Silverman77a , Mirel92]

Essentiality data for cheA 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]

Subunit of chemotaxis signaling complex - ribose/galactose/glucose sensing: CheW

Synonyms: purine-binding chemotaxis protein

Gene: cheW Accession Numbers: EG10149 (EcoCyc), b1887, ECK1888

Locations: cytosol

Sequence Length: 167 AAs

Molecular Weight [ Bairoch93]: 18.084 kD (from nucleotide sequence)

pI: 4.54

GO Terms:
Biological Process:
Inferred from experimentInferred by computational analysisGO:0006935 - chemotaxis [UniProtGOA11a, GOA01a, Liu89]
Inferred from experimentInferred by computational analysisGO:0007165 - signal transduction [GOA01a, Gegner91, Liu89]
Inferred from experimentGO:0051649 - establishment of localization in cell [Kentner06]
Molecular Function:
Inferred from experimentGO:0005515 - protein binding [Arifuzzaman06, Rajagopala09]
Inferred by computational analysisGO:0004871 - signal transducer activity [GOA01a]
Cellular Component:
Inferred from experimentGO:0005829 - cytosol [Ridgway77]
Inferred by computational analysisGO:0005737 - cytoplasm [UniProtGOA11, UniProtGOA11a]

MultiFun Terms: cell processesmotility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
regulationtype of regulationposttranscriptionalinhibition / activation of enzymes

Unification Links: DIP:DIP-48236N, EcoliWiki:b1887, Mint:MINT-1283783, ModBase:P0A964, PR:PRO_000022280, Protein Model Portal:P0A964, RefSeq:NP_416401, SMR:P0A964, UniProt:P0A964

Relationship Links: InterPro:IN-FAMILY:IPR002545, PDB:Structure:2HO9, Pfam:IN-FAMILY:PF01584, Prosite:IN-FAMILY:PS50851, Smart:IN-FAMILY:SM00260

CheW is involved in the transmission of sensory signals from the methyl-accepting chemotaxis proteins (MCPs) to the flagellar motors. CheW provides a physical coupling of CheA to the MCPs allowing regulated phosphotransfer to the CheY and CheB proteins. When CheW is complexed with CheA(L) and CheA(S) in a 1:1:1 ratio the autophosphorylation rate of CheA is increased [Bairoch93, Gegner91, Liu89, McNally91, Liu97c, Neidhardt96]. Excess levels of CheW disrupt CheA activation and chemotactic response [Liu89, Sanders89a, Boukhvalova02] possibly by disrupting the normal formation of receptor complexes [Studdert05, Cardozo10].

Citations: [Underbakke11]

Essentiality data for cheW knockouts:

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
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]

Subunit of chemotaxis signaling complex - ribose/galactose/glucose sensing: methyl accepting chemotaxis protein - ribose/galactose/glucose sensing

Synonyms: MCP-III, ribose/galactose/glucose chemoreceptor protein, Trg dimer, chemotaxis signaling protein III

Gene: trg Accession Numbers: EG11018 (EcoCyc), b1421, ECK1415

Locations: inner membrane

Subunit composition of methyl accepting chemotaxis protein - ribose/galactose/glucose sensing = [Trg]2

Map Position: [1,492,470 -> 1,494,110] (32.15 centisomes, 116°)
Length: 1641 bp / 546 aa

Molecular Weight of Polypeptide: 58.899 kD (from nucleotide sequence)

pI: 6.61

GO Terms:
Biological Process:
Inferred from experimentInferred by computational analysisGO:0006935 - chemotaxis [UniProtGOA11a, GOA01a, Kondoh79]
Inferred from experimentInferred by computational analysisGO:0007165 - signal transduction [UniProtGOA11a, GOA01a, Kondoh79, Hughson96]
Molecular Function:
Inferred from experimentInferred by computational analysisGO:0004888 - transmembrane signaling receptor activity [GOA01a, Kondoh79, Hughson96]
Inferred from experimentGO:0005515 - protein binding [Rajagopala14]
Inferred by computational analysisGO:0004871 - signal transducer activity [UniProtGOA11a, GOA01a]
Cellular Component:
Inferred from experimentInferred by computational analysisGO:0005886 - plasma membrane [UniProtGOA11, UniProtGOA11a, DiazMejia09, Zhang07, Daley05, Hazelbauer81]
Inferred by computational analysisGO:0005887 - integral component of plasma membrane [Bollinger84]
Inferred by computational analysisGO:0016020 - membrane [UniProtGOA11a, GOA01a]
Inferred by computational analysisGO:0016021 - integral component of membrane [UniProtGOA11a, GOA01a]

MultiFun Terms: cell processesmotility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
cell structuremembrane
regulationtype of regulationposttranscriptionalinhibition / activation of enzymes

Unification Links: DIP:DIP-11027N, EcoliWiki:b1421, Mint:MINT-1228342, ModBase:P05704, PR:PRO_000024111, Protein Model Portal:P05704, RefSeq:NP_415938, SMR:P05704, Swiss-Model:P05704, UniProt:P05704

Relationship Links: InterPro:IN-FAMILY:IPR003122, InterPro:IN-FAMILY:IPR003660, InterPro:IN-FAMILY:IPR004089, InterPro:IN-FAMILY:IPR004090, InterPro:IN-FAMILY:IPR004091, Pfam:IN-FAMILY:PF00015, Pfam:IN-FAMILY:PF00672, Pfam:IN-FAMILY:PF02203, Prints:IN-FAMILY:PR00260, Prosite:IN-FAMILY:PS00538, Prosite:IN-FAMILY:PS50111, Prosite:IN-FAMILY:PS50885, Smart:IN-FAMILY:SM00283, Smart:IN-FAMILY:SM00304, Smart:IN-FAMILY:SM00319

The trg gene product is one of four methyl-accepting chemotaxis proteins (MCPs) in E. coli. MCP-III is the receptor for the attractants ribose and galactose. MCP-III interacts with the periplasmic ribose- or galactose-binding proteins to mediate taxis to these attractants [Hazelbauer71, Kondoh79, Yaghmai93]. It is also thermosensitive [Nara91]. trg expressed from a plasmid in an E. coli strain lacking all four MCPs, mediates a repellent response to phenol [Yamamoto90].

E. coli Trg is a homodimeric inner membrane protein; the Trg monomer consists of a periplasmic, ligand-sensing domain, two trans-membrane segments (TM1 and TM2) and a cytoplasmic signaling domain predicted to contain 5 methylation sites [Kehry83, Nowlin87, Bollinger84, Nowlin88, Lee94]. Methylation and demethylation of MCPs in E. coli K-12 is catalysed by the CheR methyltransferase and the CheB methylesterase. Two methyl accepting residues arise from CheB catalysed post-translational deamidation of glutamines to yield glutamates [Engstrom83].

The cytoplasmic domains of the four E. coli MCPs have a high degree of sequence similarity [Krikos83, Le96, Alexander07].Trg contains a HAMP domain (present in histidine kinases, adenylate cyclases, methyl accepting chemotaxis proteins, phosphatases) which is located between the transmembrane region of the molecule and the cytoplasmic signalling region. HAMP domains are thought to mediate input/ouptut signaling (reviewed in [Parkinson10].

Trg and Tap are considered to be low-abundance receptors while Tsr and Tar are considered to be high-abundance [Hazelbauer81, Hazelbauer81a, Harayama82]

trg: taxis to ribose and galactose

Citations: [Parkinson75, Hazelbauer89 , Yang79, Lee95b, Baumgartner96, Lee95c, Hughson96, Beel01, Park86, Hazelbauer69, Adler73]

Essentiality data for trg knockouts:

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
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]


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