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Escherichia coli K-12 substr. MG1655 Enzyme: chemotaxis protein methyltransferase



Gene: cheR Accession Numbers: EG10148 (EcoCyc), b1884, ECK1885

Synonyms: cheX

Regulation Summary Diagram: ?

Summary:
CheR is a component of the adaptation pathway of the chemotaxis sensory transduction system of Escherichia coli. Adaptation allows the cell to adapt to a background stimulus so that it is capable of recognizing a concentration gradient even in the presence of a large constant level of attractant or repellent [Falke97]. A feedback loop works to control adaptation by covalently modifying a number of glutamate residues on the cytoplasmic portion of the methylatable chemotaxis protein (MCP) receptor. CheR is a methlytransferase which is transiently bound to the C terminus of the MCP receptor where it methyl esterifies the glutamate side chains, increasing the kinase activation signal of the receptor. The activity of CheR is counteracted by the methylesterase CheB, which , when phosphorylated becomes activated and hydrolyzes the methyl esters, causing a feedback reduction in the receptor's kinase activity [Falke97].

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

Locations: inner membrane, cytosol

Map Position: [1,966,528 <- 1,967,388] (42.39 centisomes)
Length: 861 bp / 286 aa

Molecular Weight of Polypeptide: 32.849 kD (from nucleotide sequence)

pI: 9.14

Unification Links: ASAP:ABE-0006286 , CGSC:926 , DIP:DIP-9273N , EchoBASE:EB0146 , EcoGene:EG10148 , EcoliWiki:b1884 , ModBase:P07364 , OU-Microarray:b1884 , PortEco:cheR , PR:PRO_000022279 , Protein Model Portal:P07364 , RefSeq:NP_416398 , RegulonDB:EG10148 , SMR:P07364 , String:511145.b1884 , Swiss-Model:P07364 , UniProt:P07364

Relationship Links: InterPro:IN-FAMILY:IPR000780 , InterPro:IN-FAMILY:IPR022641 , InterPro:IN-FAMILY:IPR022642 , InterPro:IN-FAMILY:IPR026024 , Pfam:IN-FAMILY:PF01739 , Pfam:IN-FAMILY:PF03705 , Prints:IN-FAMILY:PR00996 , Prosite:IN-FAMILY:PS50123 , Smart:IN-FAMILY:SM00138

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006479 - protein methylation Inferred by computational analysis [GOA01a]
GO:0006935 - chemotaxis Inferred by computational analysis [UniProtGOA11]
GO:0032259 - methylation Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0008168 - methyltransferase activity Inferred by computational analysis [UniProtGOA11]
GO:0008757 - S-adenosylmethionine-dependent methyltransferase activity Inferred by computational analysis [GOA01]
GO:0008983 - protein-glutamate O-methyltransferase activity Inferred by computational analysis [GOA01a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ridgway77]
GO:0005886 - plasma membrane Inferred from experiment [Ridgway77]

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

Essentiality data for cheR knockouts: ?

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

Enzymatic reaction of: chemotaxis protein methyltransferase

EC Number: 2.1.1.-

S-adenosyl-L-methionine + Tsrglu <=> S-adenosyl-L-homocysteine + Tsrglu-Me

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.


Enzymatic reaction of: chemotaxis protein methyltransferase

EC Number: 2.1.1.-

S-adenosyl-L-methionine + Trgglu <=> S-adenosyl-L-homocysteine + Trgglu-Me

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.


Enzymatic reaction of: chemotaxis protein methyltransferase

EC Number: 2.1.1.-

S-adenosyl-L-methionine + Targlu <=> S-adenosyl-L-homocysteine + Targlu-Me

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.

Inhibitors (Competitive): Targlu-Me [Neidhardt96]


Enzymatic reaction of: chemotaxis protein methyltransferase

EC Number: 2.1.1.-

S-adenosyl-L-methionine + Tapglu <=> S-adenosyl-L-homocysteine + Tapglu-Me

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.


Enzymatic reaction of: chemotaxis protein methyltransferase

Synonyms: MCP O-methyltransferase, S-adenosyl-L-methionine:protein-L-glutamate O-methyltransferase, methyl-accepting chemotaxis protein O-methyltransferase, protein-glutamate O-methyltransferase

EC Number: 2.1.1.80

a [protein]-α-L-glutamate + S-adenosyl-L-methionine <=> a [protein]-L-glutamate-O5-methyl-ester + S-adenosyl-L-homocysteine

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

Alternative Substrates [Comment 3]:

Summary:
The methyl-accepting chemotaxis proteins (MCPs) mediate chemotaxis responses in E. coli. They are reversibly methyl esterified at specific glutamate residues. The cheR encoded methyltransferase transfers methyl groups from S-adenosylmethionine (AdoMet) to those glutamate residues. Increased levels of methylation result in tumbling behavior of the cell while decreased levels result in smooth swimming. [Neidhardt96, Russell89, Hoch95]

Citations: [Pao95, Parkinson92, Stock90, Parkinson93, Hess88, Saier94]

Inhibitors (Competitive): S-adenosyl-L-homocysteine [Neidhardt96]

Primary Physiological Regulators of Enzyme Activity: S-adenosyl-L-homocysteine


Sequence Features

Feature Class Location Citations Comment
Conserved-Region 15 -> 286
[UniProt09]
UniProt: CheR-type methyltransferase;
Amino-Acid-Sites-That-Bind 92
[UniProt10a]
UniProt: S-adenosyl-L-methionine; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 94
[UniProt10a]
UniProt: S-adenosyl-L-methionine; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 98
[UniProt10a]
UniProt: S-adenosyl-L-methionine; Non-Experimental Qualifier: by similarity;
Sequence-Conflict 113
[Mutoh86, UniProt10]
Alternate sequence: R → G; UniProt: (in Ref. 1; AAA23568);
Amino-Acid-Sites-That-Bind 129
[UniProt10a]
UniProt: S-adenosyl-L-methionine; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 154
[UniProt10a]
UniProt: S-adenosyl-L-methionine; Non-Experimental Qualifier: by similarity;
Protein-Segment 212 -> 213
[UniProt10a]
UniProt: S-adenosyl-L-methionine binding; Sequence Annotation Type: region of interest; Non-Experimental Qualifier: by similarity;
Protein-Segment 230 -> 231
[UniProt10a]
UniProt: S-adenosyl-L-methionine binding; Sequence Annotation Type: region of interest; Non-Experimental Qualifier: by similarity;


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b1884 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10148; 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

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

Falke97: Falke JJ, Bass RB, Butler SL, Chervitz SA, Danielson MA (1997). "The two-component signaling pathway of bacterial chemotaxis: a molecular view of signal transduction by receptors, kinases, and adaptation enzymes." Annu Rev Cell Dev Biol 13;457-512. PMID: 9442881

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.

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

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

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

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.

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

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

Russell89: Russell CB, Stewart RC, Dahlquist FW (1989). "Control of transducer methylation levels in Escherichia coli: investigation of components essential for modulation of methylation and demethylation reactions." J Bacteriol 1989;171(7);3609-18. PMID: 2661528

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

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

Stock84: Stock JB, Clarke S, Koshland DE (1984). "The protein carboxylmethyltransferase involved in Escherichia coli and Salmonella typhimurium chemotaxis." Methods Enzymol 1984;106;310-21. PMID: 6387375

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

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

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

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

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

Liu95: 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
Page generated by SRI International Pathway Tools version 18.5 on Fri Dec 19, 2014, biocyc11.