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MetaCyc Enzyme: chemotaxis protein methyltransferase

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

Synonyms: cheX

Species: Escherichia coli K-12 substr. MG1655

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].

Locations: inner membrane, cytosol

Map Position: [1,966,528 <- 1,967,388]

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: ?

GO Terms:

Biological Process: GO:0006479 - protein methylation Inferred by computational analysis [GOA01]
GO:0006935 - chemotaxis Inferred by computational analysis [UniProtGOA11a]
GO:0032259 - methylation Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0008168 - methyltransferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0008757 - S-adenosylmethionine-dependent methyltransferase activity Inferred by computational analysis [GOA01a]
GO:0008983 - protein-glutamate O-methyltransferase activity Inferred by computational analysis [GOA01]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
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

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


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

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 1]:

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

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, Saier94a]

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
[UniProt10]
UniProt: S-adenosyl-L-methionine; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 94
[UniProt10]
UniProt: S-adenosyl-L-methionine; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 98
[UniProt10]
UniProt: S-adenosyl-L-methionine; Non-Experimental Qualifier: by similarity;
Sequence-Conflict 113
[Mutoh86, UniProt, 2010]
Alternate sequence: G; UniProt: (in Ref. 1; AAA23568);
Amino-Acid-Sites-That-Bind 129
[UniProt10]
UniProt: S-adenosyl-L-methionine; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 154
[UniProt10]
UniProt: S-adenosyl-L-methionine; Non-Experimental Qualifier: by similarity;
Protein-Segment 212 -> 213
[UniProt10]
UniProt: S-adenosyl-L-methionine binding; Sequence Annotation Type: region of interest; Non-Experimental Qualifier: by similarity;
Protein-Segment 230 -> 231
[UniProt10]
UniProt: S-adenosyl-L-methionine binding; Sequence Annotation Type: region of interest; Non-Experimental Qualifier: by similarity;

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


References

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

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

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.

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

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

Saier94a: Saier MH (1994). "Bacterial sensor kinase/response regulator systems: an introduction." Res Microbiol 1994;145(5-6);349-55. PMID: 7855419

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

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

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


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sat Nov 22, 2014, biocyc13.