Difference between revisions of "Sco"
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* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
| − | * '''Interactions:''' [[Sco]]-[[CtaC]] {{PubMed|14766920}} | + | * '''[[SubtInteract|Interactions]]:''' |
| + | ** [[Sco]]-[[CtaC]] {{PubMed|14766920}} | ||
| − | * '''Localization:''' cell membrane {{PubMed|19921776}} | + | * '''[[Localization]]:''' cell membrane {{PubMed|19921776}} |
=== Database entries === | === Database entries === | ||
| Line 131: | Line 132: | ||
=References= | =References= | ||
'''Additional publications:''' {{PubMed|21069401}} | '''Additional publications:''' {{PubMed|21069401}} | ||
| − | <pubmed>14680962, 14766920, 16305244, 19027886, 10837475 19921776 20232870 21333651 21945854</pubmed> | + | <pubmed>14680962, 14766920, 16305244, 19027886, 10837475 19921776 20232870 21333651 21945854 22036877 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 08:18, 1 November 2011
- 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 |
| 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 |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
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
- 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
- Structure: 1XZO
- UniProt: P54178
- 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
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)
