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Escherichia coli K-12 substr. MG1655 Protein: Tapglu

Subunit composition of chemotaxis signaling complex - dipeptide sensing = [(CheA)2][CheW]2[(Tap)2]3
         CheA(L) histidine kinase = (CheA)2
         methyl accepting chemotaxis protein - dipeptide sensing = (Tap)2 (extended summary available)

Alternative forms of Tapglu:
chemotaxis signaling complex - dipeptide sensing (extended summary available)
Tapglu-Me
Tapgln

Reactions known to consume the compound:

Not in pathways:
S-adenosyl-L-methionine + TapgluS-adenosyl-L-homocysteine + Tapglu-Me

Reactions known to produce the compound:

Not in pathways:
Tapglu-Me + H2O → methanol + Tapglu
Tapgln + H2O → ammonia + Tapglu

Gene-Reaction Schematic: ?


Subunit of Tapglu: 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: [1,971,384 <- 1,973,348] (42.49 centisomes)
Length: 1965 bp / 654 aa

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

pI: 4.96

GO Terms:

Biological Process: GO:0000160 - phosphorelay signal transduction system Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01, Igo89]
GO:0016310 - phosphorylation Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01, Igo89]
GO:0031400 - negative regulation of protein modification process Inferred from experiment [Barak04]
GO:0046777 - protein autophosphorylation Inferred from experiment [Igo89]
GO:0006935 - chemotaxis Inferred by computational analysis [UniProtGOA11a, GOA01]
GO:0007165 - signal transduction Inferred by computational analysis [GOA01]
GO:0018106 - peptidyl-histidine phosphorylation Inferred by computational analysis [GOA01a, GOA01]
GO:0023014 - signal transduction by phosphorylation Inferred by computational analysis [GOA01]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Thakor11, Rajagopala09, OConnor09, Hao09]
GO:0000155 - phosphorelay sensor kinase activity Inferred by computational analysis [GOA01]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0004673 - protein histidine kinase activity Inferred by computational analysis [GOA01a]
GO:0004871 - signal transducer activity Inferred by computational analysis [GOA01]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a]
GO:0016301 - kinase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016772 - transferase activity, transferring phosphorus-containing groups Inferred by computational analysis [GOA01]
Cellular Component: GO:0005829 - cytosol Inferred from experiment [Ridgway77]
GO:0005886 - plasma membrane Inferred from experiment [Ridgway77]
GO:0005622 - intracellular Inferred by computational analysis [GOA01]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA01]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
information transfer protein related posttranslational modification

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

Relationship Links: 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

Summary:
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 [Swanson93]. 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 [Swanson93a, 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 [Wang12a]. Chemotaxis receptors control kinase activity by regulating CheA domain mobility [Briegel13].

Citations: [Zhao06a, Levit02, Francis04, Morrison97, Piasta13, Garzon96, Thakor11]

Gene Citations: [Silverman77, Mirel92]

Essentiality data for cheA knockouts: ?

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

Subunit of Tapglu: 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: GO:0006935 - chemotaxis Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01, Liu89]
GO:0007165 - signal transduction Inferred from experiment Inferred by computational analysis [GOA01, Gegner91, Liu89]
GO:0051649 - establishment of localization in cell Inferred from experiment [Kentner06]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Arifuzzaman06, Rajagopala09]
GO:0004871 - signal transducer activity Inferred by computational analysis [GOA01]
Cellular Component: GO:0005829 - cytosol Inferred from experiment [Ridgway77]
GO:0005622 - intracellular Inferred by computational analysis [GOA01]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
regulation type of regulation posttranscriptional inhibition / 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 , String:511145.b1887 , UniProt:P0A964

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

Summary:
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, Liu97, Neidhardt96]. Excess levels of CheW disrupt CheA activation and chemotactic response [Liu89, Sanders89, 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 Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of Tapglu: methyl accepting chemotaxis protein - dipeptide sensing

Synonyms: Tap dimer, MCP-IV, dipeptide chemoreceptor protein, chemotaxis signaling protein IV

Gene: tap Accession Numbers: EG10987 (EcoCyc), b1885, ECK1886

Locations: inner membrane

Subunit composition of methyl accepting chemotaxis protein - dipeptide sensing = [Tap]2

Map Position: [1,967,407 <- 1,969,008] (42.4 centisomes)
Length: 1602 bp / 533 aa

Molecular Weight of Polypeptide: 57.512 kD (from nucleotide sequence), 65.0 kD (experimental) [Slocum83 ]

pI: 5.87

GO Terms:

Biological Process: GO:0006935 - chemotaxis Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01, Manson86]
GO:0007165 - signal transduction Inferred by computational analysis [UniProtGOA11a, GOA01]
Molecular Function: GO:0004871 - signal transducer activity Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01, Manson86]
GO:0004888 - transmembrane signaling receptor activity Inferred from experiment Inferred by computational analysis [GOA01, Manson86]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Zhang07, Daley05]
GO:0005887 - integral component of plasma membrane Inferred by computational analysis [Krikos83]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a, GOA01]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
cell structure membrane
regulation type of regulation posttranscriptional inhibition / activation of enzymes

Unification Links: DIP:DIP-10955N , EcoliWiki:b1885 , Mint:MINT-1309514 , ModBase:P07018 , PR:PRO_000024025 , Protein Model Portal:P07018 , RefSeq:NP_416399 , SMR:P07018 , String:511145.b1885 , Swiss-Model:P07018 , UniProt:P07018

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

Summary:
The tap gene product is one of four methyl-accepting chemotaxis proteins (MCPs) in E. coli K-12. MCP-IV interacts with the the periplasmic dipeptide-binding protein DppA to mediate taxis toward dipeptides. Dipeptides are good attractants, tripeptides are poor attractants. Peptides containing D-amino acids are poor attractants [Manson86, Abouhamad91].

E. coli Tap is predicted to be a homodimeric inner membrane protein; the Tap monomer consists of a periplasmic, ligand-sensing domain, two trans-membrane segments (TM1 and TM2) and a cytoplasmic signaling domain containing putative methylation sites [Krikos83, Le96]. Methylation and demethylation of MCPs in E. coli K-12 is catalysed by the CheR methyltransferase and the CheB methylesterase.

The cytoplasmic domains of the four E. coli MCPs have a high degree of sequence similarity [Krikos83, Le96, Alexander07]. Tap 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]. E. coli Tap is predicted to form a ternary complexe with the histidine autokinase CheA and the coupling protein CheW.

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

tap: taxis associated protein

Reviews: [Stock00, Hazelbauer08]

Citations: [Slocum85]

Gene Citations: [Kundu97, Arnosti89, Parkinson82, Parkinson78]

Essentiality data for tap knockouts: ?

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

References

Abouhamad91: Abouhamad WN, Manson M, Gibson MM, Higgins CF (1991). "Peptide transport and chemotaxis in Escherichia coli and Salmonella typhimurium: characterization of the dipeptide permease (Dpp) and the dipeptide-binding protein." Mol Microbiol 5(5);1035-47. PMID: 1956284

Alexander07: Alexander RP, Zhulin IB (2007). "Evolutionary genomics reveals conserved structural determinants of signaling and adaptation in microbial chemoreceptors." Proc Natl Acad Sci U S A 104(8);2885-90. PMID: 17299051

Arifuzzaman06: Arifuzzaman M, Maeda M, Itoh A, Nishikata K, Takita C, Saito R, Ara T, Nakahigashi K, Huang HC, Hirai A, Tsuzuki K, Nakamura S, Altaf-Ul-Amin M, Oshima T, Baba T, Yamamoto N, Kawamura T, Ioka-Nakamichi T, Kitagawa M, Tomita M, Kanaya S, Wada C, Mori H (2006). "Large-scale identification of protein-protein interaction of Escherichia coli K-12." Genome Res 16(5);686-91. PMID: 16606699

Arnosti89: Arnosti DN, Chamberlin MJ (1989). "Secondary sigma factor controls transcription of flagellar and chemotaxis genes in Escherichia coli." Proc Natl Acad Sci U S A 86(3);830-4. PMID: 2644646

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

Bairoch93: Bairoch A, Boeckmann B (1993). "The SWISS-PROT protein sequence data bank, recent developments." Nucleic Acids Res. 21:3093-3096. PMID: 8332529

Barak04: Barak R, Eisenbach M (2004). "Co-regulation of acetylation and phosphorylation of CheY, a response regulator in chemotaxis of Escherichia coli." J Mol Biol 342(2);375-81. PMID: 15327941

Bhatnagar12: Bhatnagar J, Sircar R, Borbat PP, Freed JH, Crane BR (2012). "Self-association of the histidine kinase CheA as studied by pulsed dipolar ESR spectroscopy." Biophys J 102(9);2192-201. PMID: 22824284

Borkovich89: Borkovich KA, Kaplan N, Hess JF, Simon MI (1989). "Transmembrane signal transduction in bacterial chemotaxis involves ligand-dependent activation of phosphate group transfer." Proc Natl Acad Sci U S A 86(4);1208-12. PMID: 2645576

Borkovich90: Borkovich KA, Simon MI (1990). "The dynamics of protein phosphorylation in bacterial chemotaxis." Cell 63(6);1339-48. PMID: 2261645

Boukhvalova02: Boukhvalova MS, Dahlquist FW, Stewart RC (2002). "CheW binding interactions with CheA and Tar. Importance for chemotaxis signaling in Escherichia coli." J Biol Chem 277(25);22251-9. PMID: 11923283

Bourret93: Bourret RB, Davagnino J, Simon MI (1993). "The carboxy-terminal portion of the CheA kinase mediates regulation of autophosphorylation by transducer and CheW." J Bacteriol 175(7);2097-101. PMID: 8384620

Briegel13: Briegel A, Ames P, Gumbart JC, Oikonomou CM, Parkinson JS, Jensen GJ (2013). "The mobility of two kinase domains in the Escherichia coli chemoreceptor array varies with signalling state." Mol Microbiol 89(5);831-41. PMID: 23802570

Cardozo10: Cardozo MJ, Massazza DA, Parkinson JS, Studdert CA (2010). "Disruption of chemoreceptor signalling arrays by high levels of CheW, the receptor-kinase coupling protein." Mol Microbiol 75(5);1171-81. PMID: 20487303

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

Francis04: Francis NR, Wolanin PM, Stock JB, Derosier DJ, Thomas DR (2004). "Three-dimensional structure and organization of a receptor/signaling complex." Proc Natl Acad Sci U S A 101(50);17480-5. PMID: 15572451

Garzon96: Garzon A, Parkinson JS (1996). "Chemotactic signaling by the P1 phosphorylation domain liberated from the CheA histidine kinase of Escherichia coli." J Bacteriol 178(23);6752-8. PMID: 8955292

Gegner91: Gegner JA, Dahlquist FW (1991). "Signal transduction in bacteria: CheW forms a reversible complex with the protein kinase CheA." Proc Natl Acad Sci U S A 1991;88(3);750-4. PMID: 1992467

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

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

Hao09: Hao S, Hamel D, Zhou H, Dahlquist FW (2009). "Structural basis for the localization of the chemotaxis phosphatase CheZ by CheAS." J Bacteriol 191(18);5842-4. PMID: 19502407

Harayama82: Harayama S, Engstrom P, Wolf-Watz H, Iino T, Hazelbauer GL (1982). "Cloning of trg, a gene for a sensory transducer in Escherichia coli." J Bacteriol 152(1);372-83. PMID: 6749811

Hazelbauer08: Hazelbauer GL, Falke JJ, Parkinson JS (2008). "Bacterial chemoreceptors: high-performance signaling in networked arrays." Trends Biochem Sci 33(1);9-19. PMID: 18165013

Hazelbauer81: Hazelbauer GL, Engstrom P, Harayama S (1981). "Methyl-accepting chemotaxis protein III and transducer gene trg." J Bacteriol 145(1);43-9. PMID: 7007323

Hazelbauer81a: Hazelbauer GL, Engstrom P (1981). "Multiple forms of methyl-accepting chemotaxis proteins distinguished by a factor in addition to multiple methylation." J Bacteriol 145(1);35-42. PMID: 7007319

Hess88: Hess JF, Bourret RB, Simon MI (1988). "Histidine phosphorylation and phosphoryl group transfer in bacterial chemotaxis." Nature 1988;336(6195);139-43. PMID: 3185734

Hess88a: Hess JF, Oosawa K, Kaplan N, Simon MI (1988). "Phosphorylation of three proteins in the signaling pathway of bacterial chemotaxis." Cell 1988;53(1);79-87. PMID: 3280143

Hoch95: Hoch, JA, Silhavy, TJ "Two-Component Signal Transduction." ASM Press, Washington, D.C. 1995.

Igo89: Igo MM, Ninfa AJ, Stock JB, Silhavy TJ (1989). "Phosphorylation and dephosphorylation of a bacterial transcriptional activator by a transmembrane receptor." Genes Dev 3(11);1725-34. PMID: 2558046

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

Kentner06: Kentner D, Thiem S, Hildenbeutel M, Sourjik V (2006). "Determinants of chemoreceptor cluster formation in Escherichia coli." Mol Microbiol 61(2);407-17. PMID: 16856941

Kofoid91: Kofoid EC, Parkinson JS (1991). "Tandem translation starts in the cheA locus of Escherichia coli." J Bacteriol 173(6);2116-9. PMID: 2002011

Krikos83: Krikos A, Mutoh N, Boyd A, Simon MI (1983). "Sensory transducers of E. coli are composed of discrete structural and functional domains." Cell 1983;33(2);615-22. PMID: 6305515

Kundu97: Kundu TK, Kusano S, Ishihama A (1997). "Promoter selectivity of Escherichia coli RNA polymerase sigmaF holoenzyme involved in transcription of flagellar and chemotaxis genes." J Bacteriol 179(13);4264-9. PMID: 9209042

Le96: Le Moual H, Koshland DE (1996). "Molecular evolution of the C-terminal cytoplasmic domain of a superfamily of bacterial receptors involved in taxis." J Mol Biol 261(4);568-85. PMID: 8794877

Levit02: Levit MN, Grebe TW, Stock JB (2002). "Organization of the receptor-kinase signaling array that regulates Escherichia coli chemotaxis." J Biol Chem 277(39);36748-54. PMID: 12119289

Levit96: Levit M, Liu Y, Surette M, Stock J (1996). "Active site interference and asymmetric activation in the chemotaxis protein histidine kinase CheA." J Biol Chem 271(50);32057-63. PMID: 8943256

Liu89: Liu JD, Parkinson JS (1989). "Role of CheW protein in coupling membrane receptors to the intracellular signaling system of bacterial chemotaxis." Proc Natl Acad Sci U S A 1989;86(22);8703-7. PMID: 2682657

Liu97: Liu Y, Levit M, Lurz R, Surette MG, Stock JB (1997). "Receptor-mediated protein kinase activation and the mechanism of transmembrane signaling in bacterial chemotaxis." EMBO J 1997;16(24);7231-40. PMID: 9405352

Manson86: Manson MD, Blank V, Brade G, Higgins CF (1986). "Peptide chemotaxis in E. coli involves the Tap signal transducer and the dipeptide permease." Nature 1986;321(6067);253-6. PMID: 3520334

McNally91: McNally DF, Matsumura P (1991). "Bacterial chemotaxis signaling complexes: formation of a CheA/CheW complex enhances autophosphorylation and affinity for CheY." Proc Natl Acad Sci U S A 1991;88(14);6269-73. PMID: 2068106

Mirel92: Mirel DB, Lustre VM, Chamberlin MJ (1992). "An operon of Bacillus subtilis motility genes transcribed by the sigma D form of RNA polymerase." J Bacteriol 1992;174(13);4197-204. PMID: 1624413

Morrison94: Morrison TB, Parkinson JS (1994). "Liberation of an interaction domain from the phosphotransfer region of CheA, a signaling kinase of Escherichia coli." Proc Natl Acad Sci U S A 91(12);5485-9. PMID: 8202513

Morrison97: Morrison TB, Parkinson JS (1997). "A fragment liberated from the Escherichia coli CheA kinase that blocks stimulatory, but not inhibitory, chemoreceptor signaling." J Bacteriol 179(17);5543-50. PMID: 9287011

Neidhardt96: Neidhardt FC, Curtiss III R, Ingraham JL, Lin ECC, Low Jr KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE "Escherichia coli and Salmonella, Cellular and Molecular Biology, Second Edition." American Society for Microbiology, Washington, D.C., 1996.

OConnor09: O'Connor C, Matsumura P, Campos A (2009). "The CheZ binding interface of CheAS is located in alpha-helix E." J Bacteriol 191(18);5845-8. PMID: 19581362

Parkinson10: Parkinson JS (2010). "Signaling mechanisms of HAMP domains in chemoreceptors and sensor kinases." Annu Rev Microbiol 64;101-22. PMID: 20690824

Parkinson78: Parkinson JS (1978). "Complementation analysis and deletion mapping of Escherichia coli mutants defective in chemotaxis." J Bacteriol 135(1);45-53. PMID: 353036

Parkinson82: Parkinson JS, Houts SE (1982). "Isolation and behavior of Escherichia coli deletion mutants lacking chemotaxis functions." J Bacteriol 151(1);106-13. PMID: 7045071

Piasta13: Piasta KN, Ulliman CJ, Slivka PF, Crane BR, Falke JJ (2013). "Defining a key receptor-CheA kinase contact and elucidating its function in the membrane-bound bacterial chemosensory array: a disulfide mapping and TAM-IDS Study." Biochemistry 52(22);3866-80. PMID: 23668882

Rajagopala09: Rajagopala SV, Hughes KT, Uetz P (2009). "Benchmarking yeast two-hybrid systems using the interactions of bacterial motility proteins." Proteomics 9(23);5296-302. PMID: 19834901

Ridgway77: Ridgway HG, Silverman M, Simon MI (1977). "Localization of proteins controlling motility and chemotaxis in Escherichia coli." J Bacteriol 132(2);657-65. PMID: 334749

Sanders89: Sanders DA, Mendez B, Koshland DE (1989). "Role of the CheW protein in bacterial chemotaxis: overexpression is equivalent to absence." J Bacteriol 171(11);6271-8. PMID: 2681160

Silverman77: Silverman M, Simon M (1977). "Identification of polypeptides necessary for chemotaxis in Escherichia coli." J Bacteriol 1977;130(3);1317-25. PMID: 324984

Slocum83: Slocum MK, Parkinson JS (1983). "Genetics of methyl-accepting chemotaxis proteins in Escherichia coli: organization of the tar region." J Bacteriol 155(2);565-77. PMID: 6307970

Slocum85: Slocum MK, Parkinson JS (1985). "Genetics of methyl-accepting chemotaxis proteins in Escherichia coli: null phenotypes of the tar and tap genes." J Bacteriol 163(2);586-94. PMID: 2991198

Stewart00: Stewart RC, Jahreis K, Parkinson JS (2000). "Rapid phosphotransfer to CheY from a CheA protein lacking the CheY-binding domain." Biochemistry 39(43);13157-65. PMID: 11052668

Stewart04: Stewart RC, Van Bruggen R (2004). "Association and dissociation kinetics for CheY interacting with the P2 domain of CheA." J Mol Biol 336(1);287-301. PMID: 14741223

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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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