CotA

• 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
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Interactions:

• Localization:
  • outer spore coat, more abundant at the mother cell-distal pole of the forespore PubMed

Database entries

• Structure: 2BHF (reduced form)

• UniProt: P07788

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: cotA (according to DBTBS)

• Expression browser: cotA PubMed

• Sigma factor: SigK PubMed

• Regulation:

• Regulatory mechanism:

• Additional information:
  • translation is likely to require Efp due to the presence of several consecutive proline residues PubMed

Biological materials

• Mutant:
  • 1S101 ( cotA::cat), PubMed, available at BGSC
  • 1S134 ( cotA::kan), PubMed, available at BGSC

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Martiniano Bello, Jose Correa-Basurto, Enrique Rudiño-Piñera
Simulation of the cavity-binding site of three bacterial multicopper oxidases upon complex stabilization: interactional profile and electron transference pathways.
J Biomol Struct Dyn: 2014, 32(8);1303-17
[PubMed:23859715] [WorldCat.org] [DOI] (I p)

Fabien Durand, Christian Hauge Kjaergaard, Emmanuel Suraniti, Sébastien Gounel, Ryan G Hadt, Edward I Solomon, Nicolas Mano
Bilirubin oxidase from Bacillus pumilus: a promising enzyme for the elaboration of efficient cathodes in biofuel cells.
Biosens Bioelectron: 2012, 35(1);140-146
[PubMed:22410485] [WorldCat.org] [DOI] (I p)

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)