Difference between revisions of "CheC"

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(Expression and regulation)
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===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
 +
* not essential for pellicle biofilm formation and mutant has similar fitness to the wild-type strain when competed during pellicle formation {{PubMed|26122431}}
  
 
=== Database entries ===
 
=== Database entries ===
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* '''Mutant:'''
 
* '''Mutant:'''
 
** 1A862 (no resistance), {{PubMed|7893679}}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1A862&Search=1A862 BGSC]
 
** 1A862 (no resistance), {{PubMed|7893679}}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1A862&Search=1A862 BGSC]
 +
** DS6867 (marker-less in NCIB3610) {{PubMed|25313396}}
 +
** TB189 ''amyE''::Phy-''sfgfp'' (marker-less in NCIB3610 with constitutive expressed ''sfgfp'') {{PubMed|26122431}}
 +
** TB205 ''amyE''::Phy-''mKATE2'' (marker-less in NCIB3610 with constitutive expressed ''mKATE2'') {{PubMed|26122431}}
  
 
* '''Expression vector:'''
 
* '''Expression vector:'''
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=References=
 
=References=
<pubmed>7893679,14993307,18774298,8866475,18990184,17908686,14749334,11722727,9194713, 14651647, 9657996,8157612, 15175317,17609139, 16469702, 20080618,17675386,20133180 17850253 21515776 23226535 24386445</pubmed>
+
<pubmed> 25313396, 26122431, 7893679,14993307,18774298,8866475,18990184,17908686,14749334,11722727,9194713, 14651647, 9657996,8157612, 15175317,17609139, 16469702, 20080618,17675386,20133180 17850253 21515776 23226535 24386445</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 13:53, 2 July 2015

  • Description: control of chemotaxis by interacting with CheD, CheY-P phosphatase, inhibition of CheR-mediated methylation of MCPs

Gene name cheC
Synonyms ylxJ
Essential no
Product CheY-P phosphatase
Function motility and chemotaxis
Gene expression levels in SubtiExpress: cheC
Interactions involving this protein in SubtInteract: CheC
MW, pI 22 kDa, 4.035
Gene length, protein length 627 bp, 209 aa
Immediate neighbours cheW, cheD
Sequences Protein DNA DNA_with_flanks
Genetic context
CheC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
CheC expression.png















Categories containing this gene/protein

protein modification, motility and chemotaxis

This gene is a member of the following regulons

CodY regulon, DegU regulon, SigD regulon, Spo0A regulon

The gene

Basic information

  • Locus tag: BSU16450

Phenotypes of a mutant

  • not essential for pellicle biofilm formation and mutant has similar fitness to the wild-type strain when competed during pellicle formation PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • CheY-P phosphatase
    • controls binding of CheD to chemoreceptors in response to the levels of CheY-P PubMed
  • Protein family: cheC family (according to Swiss-Prot)
  • Paralogous protein(s):FliY

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity: interaction with CheD enhances phosphatase activity towards CheY-P PubMed

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Additional information:
    • in minimal medium, CheC is present with 770 +/- 330 molecules per cell PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 152 PubMed

Biological materials

  • Mutant:
    • 1A862 (no resistance), PubMed, available at BGSC
    • DS6867 (marker-less in NCIB3610) PubMed
    • TB189 amyE::Phy-sfgfp (marker-less in NCIB3610 with constitutive expressed sfgfp) PubMed
    • TB205 amyE::Phy-mKATE2 (marker-less in NCIB3610 with constitutive expressed mKATE2) PubMed
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Theresa Hölscher, Benjamin Bartels, Yu-Cheng Lin, Ramses Gallegos-Monterrosa, Alexa Price-Whelan, Roberto Kolter, Lars E P Dietrich, Ákos T Kovács
Motility, Chemotaxis and Aerotaxis Contribute to Competitiveness during Bacterial Pellicle Biofilm Development.
J. Mol. Biol.: 2015, 427(23);3695-3708
[PubMed:26122431] [WorldCat.org] [DOI] (I p)

Rebecca A Calvo, Daniel B Kearns
FlgM is secreted by the flagellar export apparatus in Bacillus subtilis.
J. Bacteriol.: 2015, 197(1);81-91
[PubMed:25313396] [WorldCat.org] [DOI] (I p)

Serena Mordini, Cecilia Osera, Simone Marini, Francesco Scavone, Riccardo Bellazzi, Alessandro Galizzi, Cinzia Calvio
The role of SwrA, DegU and P(D3) in fla/che expression in B. subtilis.
PLoS ONE: 2013, 8(12);e85065
[PubMed:24386445] [WorldCat.org] [DOI] (I e)

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)

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)

Ruth E Silversmith
Auxiliary phosphatases in two-component signal transduction.
Curr. Opin. Microbiol.: 2010, 13(2);177-83
[PubMed:20133180] [WorldCat.org] [DOI] (I p)

Y Pazy, M A Motaleb, M T Guarnieri, N W Charon, R Zhao, R E Silversmith
Identical phosphatase mechanisms achieved through distinct modes of binding phosphoprotein substrate.
Proc. Natl. Acad. Sci. U.S.A.: 2010, 107(5);1924-9
[PubMed:20080618] [WorldCat.org] [DOI] (I p)

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)

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)

Travis J Muff, Richard M Foster, Peter J Y Liu, George W Ordal
CheX in the three-phosphatase system of bacterial chemotaxis.
J. Bacteriol.: 2007, 189(19);7007-13
[PubMed:17675386] [WorldCat.org] [DOI] (P p)

Travis J Muff, George W Ordal
Assays for CheC, FliY, and CheX as representatives of response regulator phosphatases.
Meth. Enzymol.: 2007, 423;336-48
[PubMed:17609139] [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)

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)

Michael M Saulmon, Ece Karatan, George W Ordal
Effect of loss of CheC and other adaptational proteins on chemotactic behaviour in Bacillus subtilis.
Microbiology (Reading, Engl.): 2004, 150(Pt 3);581-589
[PubMed:14993307] [WorldCat.org] [DOI] (P p)

Hendrik Szurmant, Travis J Muff, George W Ordal
Bacillus subtilis CheC and FliY are members of a novel class of CheY-P-hydrolyzing proteins in the chemotactic signal transduction cascade.
J. Biol. Chem.: 2004, 279(21);21787-92
[PubMed:14749334] [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)

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)