Difference between revisions of "CtaD"

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{{SubtiWiki regulon|[[Abh regulon]]}},
 
{{SubtiWiki regulon|[[Abh regulon]]}},
 
{{SubtiWiki regulon|[[AbrB regulon]]}},
 
{{SubtiWiki regulon|[[AbrB regulon]]}},
{{SubtiWiki regulon|[[ResD regulon]]}}
+
{{SubtiWiki regulon|[[ResD regulon]]}},
 +
[[Efp-dependent proteins]]
  
 
=The gene=
 
=The gene=
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ctaD_1561569_1563437_1 ctaD] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ctaD_1561569_1563437_1 ctaD] {{PubMed|22383849}}
  
* '''Sigma factor:'''  
+
* '''[[Sigma factor]]:'''  
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
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* '''Additional information:'''
 
* '''Additional information:'''
 +
** [[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 19:07, 29 April 2013

  • Description: cytochrome-c oxidase (subunit I)

Gene name ctaD
Synonyms
Essential no
Product cytochrome-c oxidase (subunit I)
Function respiration
Gene expression levels in SubtiExpress: ctaD
MW, pI 68 kDa, 6.985
Gene length, protein length 1866 bp, 622 aa
Immediate neighbours ctaC, ctaE
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
CtaD context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
CtaD expression.png















Categories containing this gene/protein

respiration, membrane proteins

This gene is a member of the following regulons

Abh regulon, AbrB regulon, ResD regulon, Efp-dependent proteins

The gene

Basic information

  • Locus tag: BSU14900

Phenotypes of a mutant

essential according to PubMed, non-essential according to PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: 4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O (according to Swiss-Prot)
  • Protein family: heme-copper respiratory oxidase family (according to Swiss-Prot)
  • Paralogous protein(s): QoxB

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:
    • expressed under anaerobic conditions (ResD) PubMed
  • 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

Helena B Thomaides, Ella J Davison, Lisa Burston, Hazel Johnson, David R Brown, Alison C Hunt, Jeffery Errington, Lloyd Czaplewski
Essential bacterial functions encoded by gene pairs.
J Bacteriol: 2007, 189(2);591-602
[PubMed:17114254] [WorldCat.org] [DOI] (P p)

N Azarkina, S Siletsky, V Borisov, C von Wachenfeldt, L Hederstedt, A A Konstantinov
A cytochrome bb'-type quinol oxidase in Bacillus subtilis strain 168.
J Biol Chem: 1999, 274(46);32810-7
[PubMed:10551842] [WorldCat.org] [DOI] (P p)

X Liu, H W Taber
Catabolite regulation of the Bacillus subtilis ctaBCDEF gene cluster.
J Bacteriol: 1998, 180(23);6154-63
[PubMed:9829923] [WorldCat.org] [DOI] (P p)

J van der Oost, C von Wachenfeld, L Hederstedt, M Saraste
Bacillus subtilis cytochrome oxidase mutants: biochemical analysis and genetic evidence for two aa3-type oxidases.
Mol Microbiol: 1991, 5(8);2063-72
[PubMed:1685007] [WorldCat.org] [DOI] (P p)