Sco

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  • Description: accessory lipoprotein required for assembly of the Cu(A) center of cytochrome c oxidase caa3

Gene name ypmQ
Synonyms
Essential no
Product oxidoreductase
Function maturation of cytochrome C oxidase caa3
MW, pI 21 kDa, 4.81
Gene length, protein length 579 bp, 193 aa
Immediate neighbours ypmR, ypmP
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YpmQ context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU21750

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: electron transfer to the maturing oxidase CtaC PubMed
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s): contains copper bound by two cysteines and a histidine residue PubMed
  • Effectors of protein activity:
  • Localization: cell membrane PubMed

Database entries

  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Gnana S Siluvai, Mary Mayfield, Mark J Nilges, Serena Debeer George, Ninian J Blackburn
Anatomy of a red copper center: spectroscopic identification and reactivity of the copper centers of Bacillus subtilis Sco and its Cys-to-Ala variants.
J Am Chem Soc: 2010, 132(14);5215-26
[PubMed:20232870] [WorldCat.org] [DOI] (I p)

Gnana S Siluvai, Michiko M Nakano, Mary Mayfield, Mark J Nilges, Ninian J Blackburn
H135A controls the redox activity of the Sco copper center. Kinetic and spectroscopic studies of the His135Ala variant of Bacillus subtilis Sco.
Biochemistry: 2009, 48(51);12133-44
[PubMed:19921776] [WorldCat.org] [DOI] (I p)

David E Davidson, Bruce C Hill
Stability of oxidized, reduced and copper bound forms of Bacillus subtilis Sco.
Biochim Biophys Acta: 2009, 1794(2);275-81
[PubMed:19027886] [WorldCat.org] [DOI] (P p)

Luisa Andruzzi, Michiko Nakano, Mark J Nilges, Ninian J Blackburn
Spectroscopic studies of metal binding and metal selectivity in Bacillus subtilis BSco, a Homologue of the Yeast Mitochondrial Protein Sco1p.
J Am Chem Soc: 2005, 127(47);16548-58
[PubMed:16305244] [WorldCat.org] [DOI] (P p)

Jenny Bengtsson, Claes von Wachenfeldt, Lena Winstedt, Per Nygaard, Lars Hederstedt
CtaG is required for formation of active cytochrome c oxidase in Bacillus subtilis.
Microbiology (Reading): 2004, 150(Pt 2);415-425
[PubMed:14766920] [WorldCat.org] [DOI] (P p)

Diann Andrews, Jennifer Rattenbury, Vijay Anand, Neil R Mattatall, Bruce C Hill
Expression, purification, and characterization of BsSco, an accessory protein involved in the assembly of cytochrome c oxidase in Bacillus subtilis.
Protein Expr Purif: 2004, 33(1);57-65
[PubMed:14680962] [WorldCat.org] [DOI] (P p)

N R Mattatall, J Jazairi, B C Hill
Characterization of YpmQ, an accessory protein required for the expression of cytochrome c oxidase in Bacillus subtilis.
J Biol Chem: 2000, 275(37);28802-9
[PubMed:10837475] [WorldCat.org] [DOI] (P p)

Additional publications: PubMed