Difference between revisions of "YotD"

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= [[Categories]] containing this gene/protein =
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{{SubtiWiki category|[[SP-beta prophage]]}},
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{{SubtiWiki category|[[poorly characterized/ putative enzymes]]}}
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= This gene is a member of the following [[regulons]] =
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{{SubtiWiki regulon|[[CsoR regulon]]}}
  
 
=The gene=
 
=The gene=
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= Categories containing this gene/protein =
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{{SubtiWiki category|[[SP-beta prophage]]}},
 
{{SubtiWiki category|[[poorly characterized/ putative enzymes]]}}
 
 
=The protein=
 
=The protein=
  

Revision as of 20:28, 8 December 2010

  • Description: similar to acyl-CoA synthetase

Gene name yotD
Synonyms
Essential no
Product unknown
Function unknown
MW, pI 4 kDa, 3.816
Gene length, protein length 129 bp, 43 aa
Immediate neighbours yotE, yotC
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YotD context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

SP-beta prophage, poorly characterized/ putative enzymes

This gene is a member of the following regulons

CsoR regulon

The gene

Basic information

  • Locus tag: BSU19920

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s): contains an iron-sulfur cluster
  • Effectors of protein activity:
  • Interactions:
  • Localization:

Database entries

  • Structure:
  • 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

Shashi Chillappagari, Andreas Seubert, Hein Trip, Oscar P Kuipers, Mohamed A Marahiel, Marcus Miethke
Copper stress affects iron homeostasis by destabilizing iron-sulfur cluster formation in Bacillus subtilis.
J Bacteriol: 2010, 192(10);2512-24
[PubMed:20233928] [WorldCat.org] [DOI] (I p)

Valentina Tosato, Alessandra M Albertini, Michela Zotti, Sabrina Sonda, Carlo V Bruschi
Sequence completion, identification and definition of the fengycin operon in Bacillus subtilis 168.
Microbiology (Reading): 1997, 143 ( Pt 11);3443-3450
[PubMed:9387222] [WorldCat.org] [DOI] (P p)