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 |
Contents
Categories containing this gene/protein
respiration, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU21750
Phenotypes of a mutant
Database entries
- BsubCyc: BSU21750
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- 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
- BsubCyc: BSU21750
- Structure: 1XZO
- UniProt: P54178
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Sigma factor:
- 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
Xin Yao, Diann Andrews, Bruce C Hill
Reactivity of ligand-swapped mutants of the SCO protein from Bacillus subtilis. Isomers of the CCH metal binding motif.
Biochim Biophys Acta: 2014, 1844(12);2193-202
[PubMed:25192666]
[WorldCat.org]
[DOI]
(P p)
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, Michiko Nakano, Mary Mayfield, Ninian J Blackburn
The essential role of the Cu(II) state of Sco in the maturation of the Cu(A) center of cytochrome oxidase: evidence from H135Met and H135SeM variants of the Bacillus subtilis Sco.
J Biol Inorg Chem: 2011, 16(2);285-97
[PubMed:21069401]
[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)