Sco

• 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
Gene expression levels in SubtiExpress: sco
Interactions involving this protein in SubtInteract: Sco
MW, pI	21 kDa, 4.81
Gene length, protein length	579 bp, 193 aa
Immediate neighbours	ypmR, ypmP
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

respiration, membrane proteins

The gene

Basic information

• Locus tag: BSU21750

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

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:

• Interactions:
  • Sco-CtaC PubMed

• Localization: cell membrane PubMed

Database entries

• Structure: 1XZO

• UniProt: P54178

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon:

• Expression browser: sco PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Additional publications: PubMed

Mark Lai, Katherine C Yam, Diann Andrews, Bruce C Hill
Copper binding traps the folded state of the SCO protein from Bacillus subtilis.
Biochim Biophys Acta: 2012, 1824(2);292-302
[PubMed:22036877] [WorldCat.org] [DOI] (P p)

Bruce C Hill, Diann Andrews
Differential affinity of BsSCO for Cu(II) and Cu(I) suggests a redox role in copper transfer to the Cu(A) center of cytochrome c oxidase.
Biochim Biophys Acta: 2012, 1817(6);948-54
[PubMed:21945854] [WorldCat.org] [DOI] (P p)

Brian Bennett, Bruce C Hill
Avoiding premature oxidation during the binding of Cu(II) to a dithiolate site in BsSCO. A rapid freeze-quench EPR study.
FEBS Lett: 2011, 585(6);861-4
[PubMed:21333651] [WorldCat.org] [DOI] (I p)

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)