Difference between revisions of "CotA"

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= This gene is a member of the following [[regulons]] =
 
= This gene is a member of the following [[regulons]] =
{{SubtiWiki regulon|[[SigK regulon]]}}
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{{SubtiWiki regulon|[[SigK regulon]]}},
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[[Efp-dependent proteins]]
  
 
=The gene=
 
=The gene=
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=cotA_683462_685003_-1 cotA] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=cotA_683462_685003_-1 cotA] {{PubMed|22383849}}
  
* '''Sigma factor:''' [[SigK]] {{PubMed|15699190,3135411}}
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* '''[[Sigma factor]]:''' [[SigK]] {{PubMed|15699190,3135411}}
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
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* '''Additional information:'''
 
* '''Additional information:'''
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** [[translation]] is likely to require [[Efp]] due to the presence of several consecutive proline residues {{PubMed|23239624,23239623}}
  
 
=Biological materials =
 
=Biological materials =

Revision as of 19:05, 29 April 2013

  • Description: laccase, bilirubin oxidase, spore coat protein (outer)

Gene name cotA
Synonyms pig
Essential no
Product laccase, bilirubin oxidase
Function resistance of the spore
Gene expression levels in SubtiExpress: cotA
MW, pI 58 kDa, 5.89
Gene length, protein length 1539 bp, 513 aa
Immediate neighbours yeaA, gabP
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
CotA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
CotA expression.png















Categories containing this gene/protein

sporulation proteins

This gene is a member of the following regulons

SigK regulon, Efp-dependent proteins

The gene

Basic information

  • Locus tag: BSU06300

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:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization:
    • outer spore coat, more abundant at the mother cell-distal pole of the forespore PubMed

Database entries

  • Structure: 2BHF (reduced form)
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Operon: cotA (according to DBTBS)
  • Regulation:
  • Regulatory mechanism:
  • Additional information:
    • translation is likely to require Efp due to the presence of several consecutive proline residues PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Additional publications: PubMed

Catarina S Silva, João M Damas, Zhenjia Chen, Vânia Brissos, Lígia O Martins, Cláudio M Soares, Peter F Lindley, Isabel Bento
The role of Asp116 in the reductive cleavage of dioxygen to water in CotA laccase: assistance during the proton-transfer mechanism.
Acta Crystallogr D Biol Crystallogr: 2012, 68(Pt 2);186-93
[PubMed:22281748] [WorldCat.org] [DOI] (I p)

André T Fernandes, Manuela M Pereira, Catarina S Silva, Peter F Lindley, Isabel Bento, Eduardo Pinho Melo, Lígia O Martins
The removal of a disulfide bridge in CotA-laccase changes the slower motion dynamics involved in copper binding but has no effect on the thermodynamic stability.
J Biol Inorg Chem: 2011, 16(4);641-51
[PubMed:21369750] [WorldCat.org] [DOI] (I p)

Isabel Bento, Catarina S Silva, Zhenjia Chen, Lígia O Martins, Peter F Lindley, Cláudio M Soares
Mechanisms underlying dioxygen reduction in laccases. Structural and modelling studies focusing on proton transfer.
BMC Struct Biol: 2010, 10;28
[PubMed:20822511] [WorldCat.org] [DOI] (I e)

Nirupama Gupta, Edgardo T Farinas
Directed evolution of CotA laccase for increased substrate specificity using Bacillus subtilis spores.
Protein Eng Des Sel: 2010, 23(8);679-82
[PubMed:20551082] [WorldCat.org] [DOI] (I p)

Zhenjia Chen, Paulo Durão, Catarina S Silva, Manuela M Pereira, Smilja Todorovic, Peter Hildebrandt, Isabel Bento, Peter F Lindley, Lígia O Martins
The role of Glu498 in the dioxygen reactivity of CotA-laccase from Bacillus subtilis.
Dalton Trans: 2010, 39(11);2875-82
[PubMed:20200715] [WorldCat.org] [DOI] (I p)

Daisuke Imamura, Ritsuko Kuwana, Hiromu Takamatsu, Kazuhito Watabe
Localization of proteins to different layers and regions of Bacillus subtilis spore coats.
J Bacteriol: 2010, 192(2);518-24
[PubMed:19933362] [WorldCat.org] [DOI] (I p)

Leif Steil, Mónica Serrano, Adriano O Henriques, Uwe Völker
Genome-wide analysis of temporally regulated and compartment-specific gene expression in sporulating cells of Bacillus subtilis.
Microbiology (Reading): 2005, 151(Pt 2);399-420
[PubMed:15699190] [WorldCat.org] [DOI] (P p)

M F Hullo, I Moszer, A Danchin, I Martin-Verstraete
CotA of Bacillus subtilis is a copper-dependent laccase.
J Bacteriol: 2001, 183(18);5426-30
[PubMed:11514528] [WorldCat.org] [DOI] (P p)

L Zheng, R Halberg, S Roels, H Ichikawa, L Kroos, R Losick
Sporulation regulatory protein GerE from Bacillus subtilis binds to and can activate or repress transcription from promoters for mother-cell-specific genes.
J Mol Biol: 1992, 226(4);1037-50
[PubMed:1518043] [WorldCat.org] [DOI] (P p)

K Sandman, L Kroos, S Cutting, P Youngman, R Losick
Identification of the promoter for a spore coat protein gene in Bacillus subtilis and studies on the regulation of its induction at a late stage of sporulation.
J Mol Biol: 1988, 200(3);461-73
[PubMed:3135411] [WorldCat.org] [DOI] (P p)

W Donovan, L B Zheng, K Sandman, R Losick
Genes encoding spore coat polypeptides from Bacillus subtilis.
J Mol Biol: 1987, 196(1);1-10
[PubMed:2821284] [WorldCat.org] [DOI] (P p)