Difference between revisions of "CheD"

From SubtiWiki
Jump to: navigation, search
Line 57: Line 57:
  
 
=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU16460&redirect=T BSU16460]
  
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/fla-che.html]
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/fla-che.html]
Line 99: Line 100:
  
 
=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU16460&redirect=T BSU16460]
  
 
* '''Structure:'''
 
* '''Structure:'''

Revision as of 13:44, 2 April 2014

  • Description: chemoreceptor deaminase, required for methylation of methyl-accepting chemotaxis proteins by CheR, enhances phosphatase activity of CheC, required for full McpC activity

Gene name cheD
Synonyms ylxK
Essential no
Product protein deaminase, CheC activity modulator
Function motility and chemotaxis
Gene expression levels in SubtiExpress: cheD
Interactions involving this protein in SubtInteract: CheD
MW, pI 17 kDa, 9.347
Gene length, protein length 498 bp, 166 aa
Immediate neighbours cheC, sigD
Sequences Protein DNA DNA_with_flanks
Genetic context
CheD context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
CheD expression.png















Categories containing this gene/protein

protein modification, motility and chemotaxis

This gene is a member of the following regulons

CodY regulon, SigD regulon, Spo0A regulon

The gene

Basic information

  • Locus tag: BSU16460

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • binds chemoreceptors and increases their ability to activate the kinase activity of CheA PubMed
    • Protein L-glutamine + H2O = protein L-glutamate + NH3 (according to Swiss-Prot)
    • deaminates Gln-586, Gln-593, and Gln594 in McpA PubMed
    • deaminates Gln-609 in McpC PubMed
  • Protein family: cheD family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • repressed under conditions that trigger sporulation (Spo0A) PubMed
  • Regulatory mechanism:
  • Additional information:
    • in minimal medium, CheD is present with 1,200 +/- 250 molecules per cell PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Travis J Muff, George W Ordal
The diverse CheC-type phosphatases: chemotaxis and beyond.
Mol Microbiol: 2008, 70(5);1054-61
[PubMed:18990184] [WorldCat.org] [DOI] (I p)

Christopher V Rao, George D Glekas, George W Ordal
The three adaptation systems of Bacillus subtilis chemotaxis.
Trends Microbiol: 2008, 16(10);480-7
[PubMed:18774298] [WorldCat.org] [DOI] (P p)

Original publications

___

____

Travis J Muff, George W Ordal
The CheC phosphatase regulates chemotactic adaptation through CheD.
J Biol Chem: 2007, 282(47);34120-8
[PubMed:17908686] [WorldCat.org] [DOI] (P p)

Xingjuan Chao, Travis J Muff, Sang-Youn Park, Sheng Zhang, Abiola M Pollard, George W Ordal, Alexandrine M Bilwes, Brian R Crane
A receptor-modifying deamidase in complex with a signaling phosphatase reveals reciprocal regulation.
Cell: 2006, 124(3);561-71
[PubMed:16469702] [WorldCat.org] [DOI] (P p)

Christopher J Kristich, George W Ordal
Analysis of chimeric chemoreceptors in Bacillus subtilis reveals a role for CheD in the function of the McpC HAMP domain.
J Bacteriol: 2004, 186(17);5950-5
[PubMed:15317802] [WorldCat.org] [DOI] (P p)

H Werhane, P Lopez, M Mendel, M Zimmer, G W Ordal, L M Márquez-Magaña
The last gene of the fla/che operon in Bacillus subtilis, ylxL, is required for maximal sigmaD function.
J Bacteriol: 2004, 186(12);4025-9
[PubMed:15175317] [WorldCat.org] [DOI] (P p)

Virginie Molle, Masaya Fujita, Shane T Jensen, Patrick Eichenberger, José E González-Pastor, Jun S Liu, Richard Losick
The Spo0A regulon of Bacillus subtilis.
Mol Microbiol: 2003, 50(5);1683-701
[PubMed:14651647] [WorldCat.org] [DOI] (P p)

Christopher J Kristich, George W Ordal
Bacillus subtilis CheD is a chemoreceptor modification enzyme required for chemotaxis.
J Biol Chem: 2002, 277(28);25356-62
[PubMed:12011078] [WorldCat.org] [DOI] (P p)

J R Kirby, C J Kristich, M M Saulmon, M A Zimmer, L F Garrity, I B Zhulin, G W Ordal
CheC is related to the family of flagellar switch proteins and acts independently from CheD to control chemotaxis in Bacillus subtilis.
Mol Microbiol: 2001, 42(3);573-85
[PubMed:11722727] [WorldCat.org] [DOI] (P p)

W Estacio, S S Anna-Arriola, M Adedipe, L M Márquez-Magaña
Dual promoters are responsible for transcription initiation of the fla/che operon in Bacillus subtilis.
J Bacteriol: 1998, 180(14);3548-55
[PubMed:9657996] [WorldCat.org] [DOI] (P p)

J R Kirby, C J Kristich, S L Feinberg, G W Ordal
Methanol production during chemotaxis to amino acids in Bacillus subtilis.
Mol Microbiol: 1997, 24(4);869-78
[PubMed:9194713] [WorldCat.org] [DOI] (P p)

M M Rosario, G W Ordal
CheC and CheD interact to regulate methylation of Bacillus subtilis methyl-accepting chemotaxis proteins.
Mol Microbiol: 1996, 21(3);511-8
[PubMed:8866475] [WorldCat.org] [DOI] (P p)

M M Rosario, J R Kirby, D A Bochar, G W Ordal
Chemotactic methylation and behavior in Bacillus subtilis: role of two unique proteins, CheC and CheD.
Biochemistry: 1995, 34(11);3823-31
[PubMed:7893679] [WorldCat.org] [DOI] (P p)

L M Márquez-Magaña, M J Chamberlin
Characterization of the sigD transcription unit of Bacillus subtilis.
J Bacteriol: 1994, 176(8);2427-34
[PubMed:8157612] [WorldCat.org] [DOI] (P p)