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Escherichia coli K-12 substr. MG1655 Enzyme: CheB-Pasp



Gene: cheB Accession Numbers: EG10147 (EcoCyc), b1883, ECK1884

Synonyms: protein-glutamate methylesterase-Pasp, regulatory protein domain cheB-asp-P, modified regulatory protein cheB, phospho-cheB, phosphorylated regulatory protein cheB, peptidoglutaminase II

Regulation Summary Diagram: ?

Alternative forms of CheB-Pasp: CheB (summary available)

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

Locations: cytosol

Map Position: [1,965,476 <- 1,966,525] (42.36 centisomes)
Length: 1050 bp / 349 aa

Molecular Weight: 37.468 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0006284 , CGSC:927 , EchoBASE:EB0145 , EcoGene:EG10147 , OU-Microarray:b1883 , PortEco:cheB , RefSeq:NP_416397 , RegulonDB:EG10147

Relationship Links: Pfam:IN-FAMILY:PF00072

In Paralogous Gene Group: 121 (40 members)

Reactions known to produce the compound:

Chemotactic Two-Component Signal Transduction :
CheA-P + CheB → CheA + CheB-Pasp

In Reactions of unknown directionality:

Not in pathways:
CheB-Pasp = CheB + phosphate

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Cellular Component: GO:0005829 - cytosol

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


Enzymatic reaction of: PGluMase (CheB-Pasp)

Synonyms: protein-glutamate methylesterase

EC Number: 3.1.1.-

Tapglu-Me + H2O <=> methanol + Tapglu

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 irreversible in the direction shown.


Enzymatic reaction of: PGluMase (CheB-Pasp)

Synonyms: protein-glutamate methylesterase

EC Number: 3.1.1.-

Targlu-Me + H2O <=> methanol + Targlu

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 irreversible in the direction shown.


Enzymatic reaction of: PGluMase (CheB-Pasp)

Synonyms: protein-glutamate methylesterase

EC Number: 3.1.1.-

Trgglu-Me + H2O <=> methanol + Trgglu

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 irreversible in the direction shown.


Enzymatic reaction of: PGluMase (CheB-Pasp)

Synonyms: protein-glutamate methylesterase

EC Number: 3.1.1.-

Tsrglu-Me + H2O <=> methanol + Tsrglu

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 irreversible in the direction shown.


Enzymatic reaction of: protein-glutamine glutaminase (CheB-Pasp)

EC Number: 3.5.1.-

Tsrgln + H2O <=> ammonia + Tsrglu

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 irreversible in the direction shown.


Enzymatic reaction of: protein-glutamine glutaminase (CheB-Pasp)

EC Number: 3.5.1.-

Trggln + H2O <=> ammonia + Trgglu

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 irreversible in the direction shown.


Enzymatic reaction of: protein-glutamine glutaminase (CheB-Pasp)

EC Number: 3.5.1.-

Targln + H2O <=> ammonia + Targlu

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 irreversible in the direction shown.


Enzymatic reaction of: protein-glutamine glutaminase (CheB-Pasp)

EC Number: 3.5.1.-

Tapgln + H2O <=> ammonia + Tapglu

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 irreversible in the direction shown.


Enzymatic reaction of: protein-glutamine glutaminase (CheB-Pasp)

Synonyms: protein-L-glutamine aminohydrolase, destabilase, glutaminyl-peptide glutaminase, peptidoglutaminase

EC Number: 3.5.1.44

a [protein]-L-glutamine + H2O <=> a [protein]-α-L-glutamate + ammonium

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 irreversible in the direction shown.

Summary:
The CheB protein is also responsible for the enzymatic conversion of the MCP glutamine residues to glutamate through deamidation. [Kehry83, Rollins81, Sherris81, Neidhardt96]


Enzymatic reaction of: PGluMase (CheB-Pasp)

Synonyms: protein-glutamate methylesterase, protein-L-glutamate O4-methyl-ester acylhydrolase, chemotaxis-specific methylesterase

EC Number: 3.1.1.61

a [protein]-L-glutamate-O5-methyl-ester + H2O <=> a [protein]-α-L-glutamate + methanol + H+

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 irreversible in the direction shown.

Summary:
The CheB protein consists of two distinct domains: a regulatory domain that accepts a phosphoryl group and a catalytic domain that catalyzes the demethylation and deamidation of MCPs. Protein-glutamate methylesterase is responsible for removing the methyl group from the γ-glutamyl methyl ester residues in the MCPs. The state of MCP methylation affects sensory responses and adaptations in the cell. [Hoch95, Neidhardt96, Bairoch93]

Inhibitors (Unknown Mechanism): a sulfhydryl reagent [Neidhardt96]


Sequence Features

Feature Class Location Citations Comment State
Phosphorylation-Modification 56
[UniProt10a]
UniProt: 4-aspartylphosphate; Non-Experimental Qualifier: by similarity;
Modified


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b1883 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10147; 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

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

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

Kehry83: Kehry MR, Bond MW, Hunkapiller MW, Dahlquist FW (1983). "Enzymatic deamidation of methyl-accepting chemotaxis proteins in Escherichia coli catalyzed by the cheB gene product." Proc Natl Acad Sci U S A 1983;80(12);3599-603. PMID: 6304723

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

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.

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

Rollins81: Rollins C, Dahlquist FW (1981). "The methyl-accepting chemotaxis proteins of E. coli: a repellent-stimulated, covalent modification, distinct from methylation." Cell 1981;25(2);333-40. PMID: 7026041

Sherris81: Sherris D, Parkinson JS (1981). "Posttranslational processing of methyl-accepting chemotaxis proteins in Escherichia coli." Proc Natl Acad Sci U S A 1981;78(10);6051-5. PMID: 6458812

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 2010-07 released on 2010-06-15 00:00:00." Database.

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


Report Errors or Provide Feedback
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 Sun Dec 21, 2014, biocyc14.