Escherichia coli K-12 substr. MG1655 Polypeptide: chemotaxis regulator transmitting signal to flagellar motor component

Gene: cheY Accession Numbers: EG10150 (EcoCyc), b1882, ECK1883

Synonyms: chemotaxis response regulator protein CheY

Regulation Summary Diagram: ?

Regulation summary diagram for cheY

Alternative forms of chemotaxis regulator transmitting signal to flagellar motor component:

CheY is the response regulator of the E. coli chemotactic signal transduction system. CheY undergoes two covalent modifications - phosphorylation and acetylation - both of which are believed to affect chemotaxis through interaction with the flagellar motor.

CheY is phosphorylated by the sensor kinase CheA(L) histidine kinase. In its activated state phospho-CheY interacts with the flagellar motor reversing the motion from counter-clockwise to clockwise which causes the cell to tumble. The CheZ protein accelerates the dephosphorylation of phospho-CheY thereby counteracting the tumble signal. Mg++ is required for both the phosphorylation and dephosphorylation of CheY, and is tightly bound to the protein. The metal ion requirement for the phosphorylation reaction is not Mg++ specific; for the dephosphorylation reaction the requirement is slightly more specific [Hess88, Lukat90, Sanders89, Volz91, Filimonov93, Hoch95].

Two CheY-P mutant analogs which are unable to produce clockwise flagella motion have been synthesised and resolved to 1.8 Å [McAdams08].

CheY acetylation in vitro is achieved by both acetyl-CoA synthetase and by autoacetylation with acetyl-CoA as donor [Barak04, Barak06]. CheY is highly acetylated in vivo and evidence suggests that this high level is mainly due to autoacetylation [Yan08]. The acetylated residues in CheY are lysine 91 and lysine 109 [Li10]. Acetylation activates CheY and results in clockwise rotation of the flagellar [Barak92, Ramakrishnan98]. Surface plasmon resonance measurements indicate that CheY acetylation reduces its binding to FliM - a component of the Flagellar Motor Switch Complex [Li10] although other studies suggest that there is no difference [Ramakrishnan98]. CheY mutants exhibit decreased sensitivity to chemotactic stimuli [Barak01]. The protein deacetylase CobB deacetylates CheY in vitro and in vivo and CobB null mutants show reduced response to chemotactic stimuli [Li10].

Citations: [Pao95, Parkinson92, Stock90, Parkinson93, Hess88a, Saier94, Yuan10, Fraiberg14]

Gene Citations: [Kundu97, Arnosti89, Slocum83, Parkinson82, Parkinson78]

Locations: cytosol

Map Position: [1,965,072 <- 1,965,461] (42.35 centisomes, 152°)
Length: 390 bp / 129 aa

Molecular Weight of Polypeptide: 14.097 kD (from nucleotide sequence)

pI: 5.08

Unification Links: ASAP:ABE-0006280 , CGSC:924 , DIP:DIP-48237N , EchoBASE:EB0148 , EcoGene:EG10150 , EcoliWiki:b1882 , OU-Microarray:b1882 , PortEco:cheY , PR:PRO_000022281 , Pride:P0AE67 , Protein Model Portal:P0AE67 , RegulonDB:EG10150 , SMR:P0AE67 , String:511145.b1882 , Swiss-Model:P0AE67 , UniProt:P0AE67

Relationship Links: InterPro:IN-FAMILY:IPR001789 , InterPro:IN-FAMILY:IPR011006 , PDB:Structure:1A0O , PDB:Structure:1AB5 , PDB:Structure:1AB6 , PDB:Structure:1BDJ , PDB:Structure:1C4W , PDB:Structure:1CEY , PDB:Structure:1CHN , PDB:Structure:1CYE , PDB:Structure:1D4Z , PDB:Structure:1DJM , PDB:Structure:1E6K , PDB:Structure:1E6L , PDB:Structure:1E6M , PDB:Structure:1EAY , PDB:Structure:1EHC , PDB:Structure:1F4V , PDB:Structure:1FFG , PDB:Structure:1FFS , PDB:Structure:1FFW , PDB:Structure:1FQW , PDB:Structure:1HEY , PDB:Structure:1JBE , PDB:Structure:1KMI , PDB:Structure:1MIH , PDB:Structure:1U8T , PDB:Structure:1UDR , PDB:Structure:1VLZ , PDB:Structure:1YMU , PDB:Structure:1YMV , PDB:Structure:1ZDM , PDB:Structure:2B1J , PDB:Structure:2ID7 , PDB:Structure:2ID9 , PDB:Structure:2IDM , PDB:Structure:2LP4 , PDB:Structure:3CHY , PDB:Structure:3F7N , PDB:Structure:3FFT , PDB:Structure:3FFW , PDB:Structure:3FFX , PDB:Structure:3FGZ , PDB:Structure:3MYY , PDB:Structure:3OLV , PDB:Structure:3OLW , PDB:Structure:3OLX , PDB:Structure:3OLY , PDB:Structure:3OO0 , PDB:Structure:3OO1 , PDB:Structure:3RVJ , PDB:Structure:3RVK , PDB:Structure:3RVL , PDB:Structure:3RVM , PDB:Structure:3RVN , PDB:Structure:3RVO , PDB:Structure:3RVP , PDB:Structure:3RVQ , PDB:Structure:3RVR , PDB:Structure:3RVS , PDB:Structure:5CHY , PDB:Structure:6CHY , Pfam:IN-FAMILY:PF00072 , Prosite:IN-FAMILY:PS50110 , Smart:IN-FAMILY:SM00448

In Paralogous Gene Group: 121 (40 members)

Reactions known to consume the compound:

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

Reactions known to produce the compound:

Not in pathways:
CheY-Pasp + H2O → CheY + phosphate
CheY-ac + NAD+ + H2O → CheY + 3''-O-acetyl-ADP-ribose + nicotinamide

Genetic Regulation Schematic: ?

Genetic regulation schematic for cheY

GO Terms:

Biological Process: GO:0000160 - phosphorelay signal transduction system Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01a, Hess88]
GO:0006473 - protein acetylation Inferred from experiment [Barak06]
GO:0006935 - chemotaxis Inferred from experiment Author statement Inferred by computational analysis [UniProtGOA11, Eisenbach96, Barak01]
GO:0018393 - internal peptidyl-lysine acetylation Inferred from experiment [Liarzi10]
GO:0071973 - bacterial-type flagellum-dependent cell motility Author statement [Eisenbach96]
GO:0097588 - archaeal or bacterial-type flagellum-dependent cell motility Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0000287 - magnesium ion binding Inferred from experiment [Lukat90]
GO:0005515 - protein binding Inferred from experiment [Thakor11, Oleksiuk11, Rajagopala09, Zhao02]
GO:0016407 - acetyltransferase activity Inferred from experiment [Barak06]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, LopezCampistrou05]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11a, UniProtGOA11]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)

Essentiality data for cheY 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]

Last-Curated ? 15-Apr-2010 by Mackie A , Macquarie University

Sequence Features

Protein sequence of chemotaxis regulator transmitting signal to flagellar motor component with features indicated

Feature Class Location Citations Comment State
Cleavage-of-Initial-Methionine 1
UniProt: Removed.
Chain 2 -> 129
UniProt: Chemotaxis protein cheY;
Conserved-Region 7 -> 124
UniProt: Response regulatory;
Mutagenesis-Variant 12
[Sola00, UniProt11]
UniProt: Abolishes magnesium binding.
Metal-Binding-Site 12
[Bellsolell94, UniProt11]
UniProt: Magnesium.
Metal-Binding-Site 13
UniProt: Magnesium.
Mutagenesis-Variant 13
[Sola00, UniProt11]
UniProt: No effect on magnesium binding.
4-aspartylphosphate-Modification 57
[Sanders89, Volz91, UniProt11a]
UniProt: 4-aspartylphosphate.
Mutagenesis-Variant 57
[Sola00, UniProt11]
UniProt: Abolishes magnesium binding.
Metal-Binding-Site 57
[Bellsolell94, UniProt11]
UniProt: Magnesium.
Phosphorylation-Modification 57
UniProt: 4-aspartylphosphate;
Metal-Binding-Site 59
[Bellsolell94, UniProt11]
UniProt: Magnesium; via carbonyl oxygen.
Mutagenesis-Variant 87
UniProt: Impairs chemotaxis; when associated with W-106.
Acetylation-Modification 91
N6-acetyllysine-Modification 92
[Ramakrishnan98, UniProt15]
UniProt: N6-acetyllysine.
Mutagenesis-Variant 92
[Ramakrishnan98, UniProt11]
UniProt: No effect on chemotaxis.
Acetylation-Modification 92
[Barak01, Ramakrishnan98, UniProt08]
UniProt: N6-acetyllysine;
Mutagenesis-Variant 95
I → A or V: Enhanced CW flagellar rotational signaling activity.
I → D, K or M: Loss of CW flagellar rotational signaling activity.
Mutagenesis-Variant 106
UniProt: Impairs chemotaxis; when associated with I-87.
N6-acetyllysine-Modification 109
[Ramakrishnan98, Barak92, UniProt15]
UniProt: N6-acetyllysine.
Acetylation-Modification 109
[Ramakrishnan98, Barak92, Li10]
Acetylation-Modification 109
UniProt: N6-acetyllysine;
Sequence-Conflict 113
[Mutoh86, UniProt10b]
UniProt: (in Ref. 2; AAA23570);

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram


10/20/97 Gene b1882 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10150; confirmed by SwissProt match.


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Barak01: Barak R, Eisenbach M (2001). "Acetylation of the response regulator, CheY, is involved in bacterial chemotaxis." Mol Microbiol 40(3);731-43. PMID: 11359578

Barak04: Barak R, Prasad K, Shainskaya A, Wolfe AJ, Eisenbach M (2004). "Acetylation of the chemotaxis response regulator CheY by acetyl-CoA synthetase purified from Escherichia coli." J Mol Biol 342(2);383-401. PMID: 15327942

Barak06: Barak R, Yan J, Shainskaya A, Eisenbach M (2006). "The chemotaxis response regulator CheY can catalyze its own acetylation." J Mol Biol 359(2);251-65. PMID: 16630631

Barak92: Barak R, Welch M, Yanovsky A, Oosawa K, Eisenbach M (1992). "Acetyladenylate or its derivative acetylates the chemotaxis protein CheY in vitro and increases its activity at the flagellar switch." Biochemistry 31(41);10099-107. PMID: 1390767

Bellsolell94: Bellsolell L, Prieto J, Serrano L, Coll M (1994). "Magnesium binding to the bacterial chemotaxis protein CheY results in large conformational changes involving its functional surface." J Mol Biol 238(4);489-95. PMID: 8176739

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

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Filimonov93: Filimonov VV, Prieto J, Martinez JC, Bruix M, Mateo PL, Serrano L (1993). "Thermodynamic analysis of the chemotactic protein from Escherichia coli, CheY." Biochemistry 1993;32(47);12906-21. PMID: 8251514

Fraiberg14: Fraiberg M, Afanzar O, Cassidy CK, Gabashvili A, Schulten K, Levin Y, Eisenbach M (2014). "CheY's acetylation sites responsible for generating clockwise flagellar rotation in Escherichia coli." Mol Microbiol. PMID: 25388160

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

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

Hess88: 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

Hess88a: Hess JF, Bourret RB, Simon MI (1988). "Histidine phosphorylation and phosphoryl group transfer in bacterial chemotaxis." Nature 1988;336(6195);139-43. PMID: 3185734

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

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

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

Li10: Li R, Gu J, Chen YY, Xiao CL, Wang LW, Zhang ZP, Bi LJ, Wei HP, Wang XD, Deng JY, Zhang XE (2010). "CobB regulates Escherichia coli chemotaxis by deacetylating the response regulator CheY." Mol Microbiol 76(5):1162-74. PMID: 20345663

Liarzi10: Liarzi O, Barak R, Bronner V, Dines M, Sagi Y, Shainskaya A, Eisenbach M (2010). "Acetylation represses the binding of CheY to its target proteins." Mol Microbiol 76(4);932-43. PMID: 20398208

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

Lukat90: Lukat GS, Stock AM, Stock JB (1990). "Divalent metal ion binding to the CheY protein and its significance to phosphotransfer in bacterial chemotaxis." Biochemistry 1990;29(23);5436-42. PMID: 2201404

McAdams08: McAdams K, Casper ES, Matthew Haas R, Santarsiero BD, Eggler AL, Mesecar A, Halkides CJ (2008). "The structures of T87I phosphono-CheY and T87I/Y106W phosphono-CheY help to explain their binding affinities to the FliM and CheZ peptides." Arch Biochem Biophys 479(2);105-13. PMID: 18801331

Mutoh86: Mutoh N, Simon MI (1986). "Nucleotide sequence corresponding to five chemotaxis genes in Escherichia coli." J Bacteriol 165(1);161-6. PMID: 3510184

Oleksiuk11: Oleksiuk O, Jakovljevic V, Vladimirov N, Carvalho R, Paster E, Ryu WS, Meir Y, Wingreen NS, Kollmann M, Sourjik V (2011). "Thermal robustness of signaling in bacterial chemotaxis." Cell 145(2);312-21. PMID: 21496648

Pao95: Pao GM, Saier MH (1995). "Response regulators of bacterial signal transduction systems: selective domain shuffling during evolution." J Mol Evol 1995;40(2);136-54. PMID: 7699720

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

Parkinson92: Parkinson JS, Kofoid EC (1992). "Communication modules in bacterial signaling proteins." Annu Rev Genet 1992;26;71-112. PMID: 1482126

Parkinson93: Parkinson JS (1993). "Signal transduction schemes of bacteria." Cell 1993;73(5);857-71. PMID: 8098993

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

Ramakrishnan98: Ramakrishnan R, Schuster M, Bourret RB (1998). "Acetylation at Lys-92 enhances signaling by the chemotaxis response regulator protein CheY." Proc Natl Acad Sci U S A 1998;95(9);4918-23. PMID: 9560203

Saier94: Saier MH (1994). "Bacterial sensor kinase/response regulator systems: an introduction." Res Microbiol 1994;145(5-6);349-55. PMID: 7855419

Sanders89: Sanders DA, Gillece-Castro BL, Stock AM, Burlingame AL, Koshland DE (1989). "Identification of the site of phosphorylation of the chemotaxis response regulator protein, CheY." J Biol Chem 1989;264(36);21770-8. PMID: 2689446

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

Sola00: Sola M, Lopez-Hernandez E, Cronet P, Lacroix E, Serrano L, Coll M, Parraga A (2000). "Towards understanding a molecular switch mechanism: thermodynamic and crystallographic studies of the signal transduction protein CheY." J Mol Biol 303(2);213-25. PMID: 11023787

Stock90: Stock JB, Stock AM, Mottonen JM (1990). "Signal transduction in bacteria." Nature 1990;344(6265);395-400. PMID: 2157156

Thakor11: Thakor H, Nicholas S, Porter IM, Hand N, Stewart RC (2011). "Identification of an anchor residue for CheA-CheY interactions in the chemotaxis system of Escherichia coli." J Bacteriol 193(15);3894-903. PMID: 21642453

UniProt08: UniProt Consortium (2008). "UniProt version 14.6 released on 2008-12-16." Database.

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt10b: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProt11a: UniProt Consortium (2011). "UniProt version 2011-11 released on 2011-11-22 00:00:00." Database.

UniProt15: UniProt Consortium (2015). "UniProt version 2015-01 released on 2015-01-16 00:00:00." Database.

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

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

Volz91: Volz K, Matsumura P (1991). "Crystal structure of Escherichia coli CheY refined at 1.7-A resolution." J Biol Chem 1991;266(23);15511-9. PMID: 1869568

Yan08: Yan J, Barak R, Liarzi O, Shainskaya A, Eisenbach M (2008). "In vivo acetylation of CheY, a response regulator in chemotaxis of Escherichia coli." J Mol Biol 376(5);1260-71. PMID: 18234227

Yuan10: Yuan J, Fahrner KA, Turner L, Berg HC (2010). "Asymmetry in the clockwise and counterclockwise rotation of the bacterial flagellar motor." Proc Natl Acad Sci U S A 107(29);12846-9. PMID: 20615986

Zhao02: Zhao R, Collins EJ, Bourret RB, Silversmith RE (2002). "Structure and catalytic mechanism of the E. coli chemotaxis phosphatase CheZ." Nat Struct Biol 9(8);570-5. PMID: 12080332

Other References Related to Gene Regulation

Constantinidou06: Constantinidou C, Hobman JL, Griffiths L, Patel MD, Penn CW, Cole JA, Overton TW (2006). "A reassessment of the FNR regulon and transcriptomic analysis of the effects of nitrate, nitrite, NarXL, and NarQP as Escherichia coli K12 adapts from aerobic to anaerobic growth." J Biol Chem 281(8);4802-15. PMID: 16377617

Helmann87: Helmann JD, Chamberlin MJ (1987). "DNA sequence analysis suggests that expression of flagellar and chemotaxis genes in Escherichia coli and Salmonella typhimurium is controlled by an alternative sigma factor." Proc Natl Acad Sci U S A 84(18);6422-4. PMID: 3306678

Ide99: Ide N, Ikebe T, Kutsukake K (1999). "Reevaluation of the promoter structure of the class 3 flagellar operons of Escherichia coli and Salmonella." Genes Genet Syst 74(3);113-6. PMID: 10586520

Ko00a: Ko M, Park C (2000). "Two novel flagellar components and H-NS are involved in the motor function of Escherichia coli." J Mol Biol 303(3);371-82. PMID: 11031114

Liu95a: Liu X, Matsumura P (1995). "An alternative sigma factor controls transcription of flagellar class-III operons in Escherichia coli: gene sequence, overproduction, purification and characterization." Gene 164(1);81-4. PMID: 7590326

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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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