Difference between revisions of "ResA"

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= [[Categories]] containing this gene/protein =
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{{SubtiWiki category|[[respiration]]}},
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{{SubtiWiki category|[[essential genes]]}}
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= This gene is a member of the following [[regulons]] =
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{{SubtiWiki regulon|[[CcpA regulon]]}},
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{{SubtiWiki regulon|[[PhoP regulon]]}},
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{{SubtiWiki regulon|[[ResD regulon]]}}
  
 
=The gene=
 
=The gene=
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= Categories containing this gene/protein =
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{{SubtiWiki category|[[respiration]]}},
 
{{SubtiWiki category|[[essential genes]]}}
 
 
=The protein=
 
=The protein=
  

Revision as of 20:58, 8 December 2010

  • Description: extracytoplasmic thioredoxin, cytochrome c biogenesis, reduces disulfide bonds in apo-cytochrome prior to the attachment of heme

Gene name resA
Synonyms ypxA
Essential yes PubMed
Product extracytoplasmic thioredoxin
Function cytochrome c biogenesis
MW, pI 20 kDa, 8.37
Gene length, protein length 543 bp, 181 aa
Immediate neighbours resB, rluB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
ResA context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

respiration, essential genes

This gene is a member of the following regulons

CcpA regulon, PhoP regulon, ResD regulon

The gene

Basic information

  • Locus tag: BSU23150

Phenotypes of a mutant

essential PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: ResA subfamily (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization:

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • expressed under anaerobic conditions (ResD) PubMed
    • expressed under conditions of phosphate limitation (PhoP) PubMed
    • repressed by glucose (CcpA) PubMed
  • 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

Christopher T C Hodson, Allison Lewin, Lars Hederstedt, Nick E Le Brun
The active-site cysteinyls and hydrophobic cavity residues of ResA are important for cytochrome c maturation in Bacillus subtilis.
J Bacteriol: 2008, 190(13);4697-705
[PubMed:18456809] [WorldCat.org] [DOI] (I p)

Allison Lewin, Allister Crow, Christopher T C Hodson, Lars Hederstedt, Nick E Le Brun
Effects of substitutions in the CXXC active-site motif of the extracytoplasmic thioredoxin ResA.
Biochem J: 2008, 414(1);81-91
[PubMed:18422485] [WorldCat.org] [DOI] (I p)

Allison Lewin, Allister Crow, Arthur Oubrie, Nick E Le Brun
Molecular basis for specificity of the extracytoplasmic thioredoxin ResA.
J Biol Chem: 2006, 281(46);35467-77
[PubMed:16971393] [WorldCat.org] [DOI] (P p)

Soo-Keun Choi, Milton H Saier
Mechanism of CcpA-mediated glucose repression of the resABCDE operon of Bacillus subtilis.
J Mol Microbiol Biotechnol: 2006, 11(1-2);104-10
[PubMed:16825793] [WorldCat.org] [DOI] (P p)

M M Nakano, Y Zhu
Involvement of ResE phosphatase activity in down-regulation of ResD-controlled genes in Bacillus subtilis during aerobic growth.
J Bacteriol: 2001, 183(6);1938-44
[PubMed:11222591] [WorldCat.org] [DOI] (P p)

S M Birkey, W Liu, X Zhang, M F Duggan, F M Hulett
Pho signal transduction network reveals direct transcriptional regulation of one two-component system by another two-component regulator: Bacillus subtilis PhoP directly regulates production of ResD.
Mol Microbiol: 1998, 30(5);943-53
[PubMed:9988472] [WorldCat.org] [DOI] (P p)

G Sun, E Sharkova, R Chesnut, S Birkey, M F Duggan, A Sorokin, P Pujic, S D Ehrlich, F M Hulett
Regulators of aerobic and anaerobic respiration in Bacillus subtilis.
J Bacteriol: 1996, 178(5);1374-85
[PubMed:8631715] [WorldCat.org] [DOI] (P p)

  • Additional publications

PubMed