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Escherichia coli K-12 substr. MG1655 Protein: CheZ



Gene: cheZ Accession Numbers: EG10151 (EcoCyc), b1881, ECK1882

Synonyms: chemotaxis protein CheZ

Regulation Summary Diagram: ?

Subunit composition of CheZ = [CheZ]2

Summary:
CheZ is a cytosolic phosphatase which functions in the chemotaxis signal transduction complex. CheY is the response regulator and a component of the two-component signal transduction complex (along with histidine kinase CheA). CheA senses changes in environmental concentrations of attractants and repellants and couples these changes through His-Asp phosphoryl shuttling to CheY. CheY-P is capable of binding to flagellar switch protein FliM and affecting swimming behavior [Welch93]. CheZ accelerates the decay of the CheY-P aspartyl-phosphate residue [Hess87], thereby helping to maintain the steady-state conditions at a level that generates a random walk swimming behavior [Manson98].

CheZ controls the level of phosphorylated CheY through dephosphorylation. It is not clear whether CheZ acts catalytically as a phosphatase or as an allosteric effector, causing a change in CheY conformation. Phospho-CheY is known to dephosphorylate spontaneously and this is further enhanced in the presence of CheZ. The CheZ protein binds more readily to phospho-CheY than CheY. The dimeric form of CheZ undergoes further oligomerization upon interaction with phospho-CheY. Additionally CheZ complexes with CheA(S) which results in enhanced dephosphorylation activity on phospho-CheY [Blat96, Sanna96, Wang96c, Blat94, Blat96a, Blat96b, Sanna96a, Sanna95, Bren96, McNamara97]. CheZ interacts with CheA(S) to localise CheZ to the cell poles [Cantwell03, Hao09].

Citations: [vanAlbada09]

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

Locations: inner membrane, cytosol, cell projection

Map Position: [1,964,417 <- 1,965,061] (42.34 centisomes)
Length: 645 bp / 214 aa

Molecular Weight of Polypeptide: 23.976 kD (from nucleotide sequence)

pI: 4.71

Unification Links: ASAP:ABE-0006278 , CGSC:923 , DIP:DIP-47931N , EchoBASE:EB0149 , EcoGene:EG10151 , EcoliWiki:b1881 , Mint:MINT-1264225 , ModBase:P0A9H9 , OU-Microarray:b1881 , PortEco:cheZ , PR:PRO_000022282 , Pride:P0A9H9 , Protein Model Portal:P0A9H9 , RefSeq:NP_416395 , RegulonDB:EG10151 , SMR:P0A9H9 , String:511145.b1881 , UniProt:P0A9H9

Relationship Links: InterPro:IN-FAMILY:IPR007439 , PDB:Structure:1KMI , Pfam:IN-FAMILY:PF04344

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0016311 - dephosphorylation Inferred by computational analysis Inferred from experiment [Wang96c, UniProtGOA11]
GO:0071945 - regulation of bacterial-type flagellum-dependent cell motility by regulation of motor speed Inferred from experiment [Wang96c]
GO:0071977 - bacterial-type flagellum-dependent swimming motility Inferred from experiment [Jeng86]
GO:0006935 - chemotaxis Inferred by computational analysis [UniProtGOA11]
GO:0008152 - metabolic process Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0050920 - regulation of chemotaxis Inferred by computational analysis [GOA01]
GO:0097588 - archaeal or bacterial-type flagellum-dependent cell motility Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0004721 - phosphoprotein phosphatase activity Inferred from experiment Inferred by computational analysis [UniProtGOA11, Wang96c]
GO:0005515 - protein binding Inferred from experiment [Oleksiuk11, Rajagopala09, OConnor09, Hao09, Zhao02a]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005829 - cytosol Inferred from experiment [Ridgway77]
GO:0005886 - plasma membrane Inferred from experiment [Ridgway77]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11a, UniProtGOA11]
GO:0009288 - bacterial-type flagellum Inferred by computational analysis [GOA01]

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

Essentiality data for cheZ 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]

Sequence Features

Feature Class Location Citations Comment
Mutagenesis-Variant 21
[Silversmith08, UniProt11]
Alternate sequence: I → T; UniProt: Gain of function, increased counterclockwise rotation of flagella.
Mutagenesis-Variant 65
[Boesch00, UniProt11]
Alternate sequence: A → V; UniProt: Loss of function, fails to oligomerize.
Mutagenesis-Variant 90
[Cantwell03, Boesch00, UniProt11]
Alternate sequence: L → S; UniProt: Loss of localization to the cell pole. Fails to oligomerize.
Mutagenesis-Variant 94
[Cantwell03, UniProt11]
Alternate sequence: W → R; UniProt: Loss of localization to the cell pole.
Mutagenesis-Variant 117
[Cantwell03, Boesch00, UniProt11]
Alternate sequence: F → S; UniProt: Loss of localization to the cell pole.
Sequence-Conflict 119
[Mutoh86, UniProt10a]
Alternate sequence: A → P; UniProt: (in Ref. 1; AAA23571);
Sequence-Conflict 130
[Mutoh86, UniProt10a]
Alternate sequence: A → G; UniProt: (in Ref. 1; AAA23571);
Mutagenesis-Variant 143
[Boesch00, UniProt11]
Alternate sequence: D → G; UniProt: Loss of function. Fails to oligomerize.
Mutagenesis-Variant 147
[Zhao02a, UniProt11]
Alternate sequence: Q → A; UniProt: Severely diminished function, exclusive clockwise flagellar rotation.
Amino-Acid-Site 147
[UniProt10a]
UniProt: Enhances dephosphorylation of CheY-P; Sequence Annotation Type: site;
Mutagenesis-Variant 188
[Boesch00, UniProt11]
Alternate sequence: G → E; UniProt: Diminished ability to stimulate dephosphorylation of CheY-P.
Mutagenesis-Variant 205
[Boesch00, UniProt11]
Alternate sequence: V → E; UniProt: Severely impairs the interaction the interaction with CheY-P.


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b1881 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10151; confirmed by SwissProt match.


References

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

Blat94: Blat Y, Eisenbach M (1994). "Phosphorylation-dependent binding of the chemotaxis signal molecule CheY to its phosphatase, CheZ." Biochemistry 1994;33(4);902-6. PMID: 8305438

Blat96: Blat Y, Eisenbach M (1996). "Oligomerization of the phosphatase CheZ upon interaction with the phosphorylated form of CheY. The signal protein of bacterial chemotaxis." J Biol Chem 1996;271(2);1226-31. PMID: 8557654

Blat96a: Blat Y, Eisenbach M (1996). "Conserved C-terminus of the phosphatase CheZ is a binding domain for the chemotactic response regulator CheY." Biochemistry 1996;35(18);5679-83. PMID: 8639527

Blat96b: Blat Y, Eisenbach M (1996). "Mutants with defective phosphatase activity show no phosphorylation-dependent oligomerization of CheZ. The phosphatase of bacterial chemotaxis." J Biol Chem 1996;271(2);1232-6. PMID: 8557655

Boesch00: Boesch KC, Silversmith RE, Bourret RB (2000). "Isolation and characterization of nonchemotactic CheZ mutants of Escherichia coli." J Bacteriol 182(12);3544-52. PMID: 10852888

Bren96: Bren A, Welch M, Blat Y, Eisenbach M (1996). "Signal termination in bacterial chemotaxis: CheZ mediates dephosphorylation of free rather than switch-bound CheY." Proc Natl Acad Sci U S A 1996;93(19);10090-3. PMID: 8816756

Cantwell03: Cantwell BJ, Draheim RR, Weart RB, Nguyen C, Stewart RC, Manson MD (2003). "CheZ phosphatase localizes to chemoreceptor patches via CheA-short." J Bacteriol 185(7);2354-61. PMID: 12644507

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."

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

Hess87: Hess JF, Oosawa K, Matsumura P, Simon MI (1987). "Protein phosphorylation is involved in bacterial chemotaxis." Proc Natl Acad Sci U S A 1987;84(21);7609-13. PMID: 3313398

Jeng86: Jeng AY, Sharkey NA, Blumberg PM (1986). "Purification of stable protein kinase C from mouse brain cytosol by specific ligand elution using fast protein liquid chromatography." Cancer Res 46(4 Pt 2);1966-71. PMID: 3456269

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

Manson98: Manson MD, Armitage JP, Hoch JA, Macnab RM (1998). "Bacterial locomotion and signal transduction." J Bacteriol 180(5);1009-22. PMID: 9495737

McNamara97: McNamara BP, Wolfe AJ (1997). "Coexpression of the long and short forms of CheA, the chemotaxis histidine kinase, by members of the family Enterobacteriaceae." J Bacteriol 1997;179(5);1813-8. PMID: 9045846

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

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

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

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

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

Sanna95: Sanna MG, Swanson RV, Bourret RB, Simon MI (1995). "Mutations in the chemotactic response regulator, CheY, that confer resistance to the phosphatase activity of CheZ." Mol Microbiol 1995;15(6);1069-79. PMID: 7623663

Sanna96: Sanna MG, Simon MI (1996). "In vivo and in vitro characterization of Escherichia coli protein CheZ gain- and loss-of-function mutants." J Bacteriol 1996;178(21);6275-80. PMID: 8892829

Sanna96a: Sanna MG, Simon MI (1996). "Isolation and in vitro characterization of CheZ suppressors for the Escherichia coli chemotactic response regulator mutant CheYN23D." J Biol Chem 1996;271(13);7357-61. PMID: 8631757

Silversmith08: Silversmith RE, Levin MD, Schilling E, Bourret RB (2008). "Kinetic characterization of catalysis by the chemotaxis phosphatase CheZ. Modulation of activity by the phosphorylated CheY substrate." J Biol Chem 283(2);756-65. PMID: 17998207

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

UniProt10a: 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.

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."

vanAlbada09: van Albada SB, Ten Wolde PR (2009). "Differential affinity and catalytic activity of CheZ in E. coli chemotaxis." PLoS Comput Biol 5(5);e1000378. PMID: 19424426

Wang96c: Wang H, Matsumura P (1996). "Characterization of the CheAS/CheZ complex: a specific interaction resulting in enhanced dephosphorylating activity on CheY-phosphate." Mol Microbiol 1996;19(4);695-703. PMID: 8820640

Welch93: Welch M, Oosawa K, Aizawa S, Eisenbach M (1993). "Phosphorylation-dependent binding of a signal molecule to the flagellar switch of bacteria." Proc Natl Acad Sci U S A 90(19);8787-91. PMID: 8415608

Zhao02a: 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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