Difference between revisions of "CheD"
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− | * '''Description:''' | + | * '''Description:''' chemoreceptor deaminase, required for methylation of methyl-accepting chemotaxis proteins by [[CheR]], enhances phosphatase activity of [[CheC]], required for full [[McpC]] activity <br/><br/> |
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
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* '''Catalyzed reaction/ biological activity:''' | * '''Catalyzed reaction/ biological activity:''' | ||
+ | ** binds chemoreceptors and increases their ability to activate the kinase activity of [[CheA]] {{PubMed|23226535}} | ||
** Protein L-glutamine + H<sub>2</sub>O = protein L-glutamate + NH<sub>3</sub> (according to Swiss-Prot) | ** Protein L-glutamine + H<sub>2</sub>O = protein L-glutamate + NH<sub>3</sub> (according to Swiss-Prot) | ||
** deaminates Gln-586, Gln-593, and Gln594 in [[McpA]] {{PubMed|22931217}} | ** deaminates Gln-586, Gln-593, and Gln594 in [[McpA]] {{PubMed|22931217}} | ||
Line 91: | Line 92: | ||
* '''[[SubtInteract|Interactions]]:''' | * '''[[SubtInteract|Interactions]]:''' | ||
− | ** [[CheC]]-[[CheD]] {{PubMed|17908686}} | + | ** [[CheC]]-[[CheD]] {{PubMed|17908686}}, this interaction is enhanced by [[CheY]]-P {{PubMed|23226535}} |
** [[CheD]]-[[McpA]], deamination of Gln-586, Gln-593 and Gln-594 in [[McpA]] {{PubMed|22931217}} | ** [[CheD]]-[[McpA]], deamination of Gln-586, Gln-593 and Gln-594 in [[McpA]] {{PubMed|22931217}} | ||
** [[CheD]]-[[McpC]], deamination of Gln-609 in [[McpC]] {{PubMed|22931217}} | ** [[CheD]]-[[McpC]], deamination of Gln-609 in [[McpC]] {{PubMed|22931217}} | ||
Line 155: | Line 156: | ||
<pubmed>,18774298,,18990184</pubmed> | <pubmed>,18774298,,18990184</pubmed> | ||
==Original publications== | ==Original publications== | ||
− | <pubmed>7893679,15317802,17908686,12011078,8866475,11722727,9194713,14651647, 9657996,8157612,15175317,16469702 17850253 21515776 22931217</pubmed> | + | <pubmed>7893679,15317802,17908686,12011078,8866475,11722727,9194713,14651647, 9657996,8157612,15175317,16469702 17850253 21515776 22931217 23226535</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 14:54, 3 January 2013
- 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 |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
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:
- 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:
- UniProt: P40404
- KEGG entry: [3]
- E.C. number: 3.5.1.44
Additional information
Expression and regulation
- Operon:
- Regulatory mechanism:
- Additional information:
- in minimal medium, CheD is present with 1,200 +/- 250 molecules per cell PubMed
Biological materials
- 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
Wei Yuan, George D Glekas, George M Allen, Hanna E Walukiewicz, Christopher V Rao, George W Ordal
The importance of the interaction of CheD with CheC and the chemoreceptors compared to its enzymatic activity during chemotaxis in Bacillus subtilis.
PLoS One: 2012, 7(12);e50689
[PubMed:23226535]
[WorldCat.org]
[DOI]
(I p)
George D Glekas, Matthew J Plutz, Hanna E Walukiewicz, George M Allen, Christopher V Rao, George W Ordal
Elucidation of the multiple roles of CheD in Bacillus subtilis chemotaxis.
Mol Microbiol: 2012, 86(3);743-56
[PubMed:22931217]
[WorldCat.org]
[DOI]
(I p)
Vincent J Cannistraro, George D Glekas, Christopher V Rao, George W Ordal
Cellular stoichiometry of the chemotaxis proteins in Bacillus subtilis.
J Bacteriol: 2011, 193(13);3220-7
[PubMed:21515776]
[WorldCat.org]
[DOI]
(I p)
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)
Kazuo Kobayashi
Gradual activation of the response regulator DegU controls serial expression of genes for flagellum formation and biofilm formation in Bacillus subtilis.
Mol Microbiol: 2007, 66(2);395-409
[PubMed:17850253]
[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)