Difference between revisions of "Sco"

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* '''Description:''' maturation of cytochrom C oxidase caa3 <br/><br/>
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* '''Description:''' accessory lipoprotein required for assembly of the Cu(A) center of cytochrome c oxidase caa3 <br/><br/>
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
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|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"| '''Product''' || unknown
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|style="background:#ABCDEF;" align="center"| '''Product''' || oxidoreductase
 
|-
 
|-
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|style="background:#ABCDEF;" align="center"|'''Function''' || maturation of cytochrom C oxidase caa3
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|style="background:#ABCDEF;" align="center"|'''Function''' || maturation of cytochrome C oxidase caa3
 +
|-
 +
|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU21750 sco]
 +
|-
 +
|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://subtiwiki.uni-goettingen.de/interact/ ''Subt''Interact]''': [http://subtiwiki.uni-goettingen.de/interact/index.php?protein=Sco Sco]
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 21 kDa, 4.81   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 21 kDa, 4.81   
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ypmR]]'', ''[[ypmP]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ypmR]]'', ''[[ypmP]]''
 
|-
 
|-
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|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB14093&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU21750 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU21750 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU21750 DNA_with_flanks]
 
|-
 
|-
 
|-
 
|-
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|colspan="2" | '''Genetic context''' <br/> [[Image:ypmQ_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:ypmQ_context.gif]]
 
  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 
  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 +
|-
 +
|colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=scuA_2291703_2292284_-1 Expression at a glance]'''&#160;&#160;&#160;{{PubMed|22383849}}<br/>[[Image:sco_expression.png|500px|link=http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU21750]]
 
|-
 
|-
 
|}
 
|}
  
 
__TOC__
 
__TOC__
 +
<br/><br/><br/><br/>
 +
<br/><br/><br/><br/>
 +
<br/><br/><br/><br/>
 +
<br/><br/>
 +
 +
= [[Categories]] containing this gene/protein =
 +
{{SubtiWiki category|[[respiration]]}},
 +
{{SubtiWiki category|[[membrane proteins]]}}
 +
 +
= This gene is a member of the following [[regulons]] =
  
−
<br/><br/>
 
  
 
=The gene=
 
=The gene=
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=== Basic information ===
 
=== Basic information ===
  
−
* '''Coordinates:'''
+
* '''Locus tag:''' BSU21750
  
 
===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
  
 
=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU21750&redirect=T BSU21750]
  
 
* '''DBTBS entry:''' no entry
 
* '''DBTBS entry:''' no entry
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=== Additional information===
 
=== Additional information===
 +
 +
  
  
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=== Basic information/ Evolution ===
 
=== Basic information/ Evolution ===
  
−
* '''Catalyzed reaction/ biological activity:'''  
+
* '''Catalyzed reaction/ biological activity:''' electron transfer to the maturing oxidase [[CtaC]] {{PubMed|19921776}}
  
 
* '''Protein family:'''
 
* '''Protein family:'''
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* '''Modification:'''
 
* '''Modification:'''
  
−
* '''Cofactor(s):'''
+
* '''Cofactor(s):''' contains copper bound by two cysteines and a histidine residue {{PubMed|19921776}}
  
 
* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
  
−
* '''Interactions:'''
+
* '''[[SubtInteract|Interactions]]:'''
 +
** [[Sco]]-[[CtaC]] {{PubMed|14766920}}
  
−
* '''Localization:'''
+
* '''[[Localization]]:''' cell membrane  {{PubMed|19921776}}
  
 
=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU21750&redirect=T BSU21750]
  
−
* '''Structure:'''
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* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1XZO 1XZO]
  
−
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P54178 P54178]
+
* '''UniProt:''' [http://www.uniprot.org/uniprot/P54178 P54178]
  
−
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU21750]
+
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU21750]
  
 
* '''E.C. number:'''
 
* '''E.C. number:'''
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* '''Operon:'''  
 
* '''Operon:'''  
  
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* '''[[Sigma factor]]:'''  
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=scuA_2291703_2292284_-1 sco] {{PubMed|22383849}}
 +
 
 +
* '''Sigma factor:'''  
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
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* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
  
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* '''Additional information:'''  
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* '''Additional information:'''
  
 
=Biological materials =
 
=Biological materials =
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=References=
 
=References=
−
 
+
<pubmed>14680962, 14766920, 16305244, 19027886, 10837475 19921776 20232870 21333651 21945854 22036877 25192666 21069401</pubmed>
−
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]
+
 +
[[Category:Protein-coding genes]]

Latest revision as of 09:29, 19 September 2014

  • 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
YpmQ context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Sco expression.png















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

  • 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:

Database entries

  • 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)

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