Difference between revisions of "YbfM"

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= Categories containing this gene/protein =
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{{SubtiWiki category|[[cell envelope stress proteins (controlled by SigM, W, X, Y)]]}},
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{{SubtiWiki category|[[membrane proteins]]}},
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{{SubtiWiki category|[[poorly characterized/ putative enzymes]]}}
 
=The protein=
 
=The protein=
  

Revision as of 21:01, 30 November 2010

  • Description: similar to alkaline phosphatase

Gene name ybfM
Synonyms
Essential no
Product unknown
Function unknown
Metabolic function and regulation of this protein in SubtiPathways:
Lipid synthesis
MW, pI 18 kDa, 9.482
Gene length, protein length 486 bp, 162 aa
Immediate neighbours pssA, psd
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YbfM context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU02280

Phenotypes of a mutant

Database entries

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

Additional information

Categories containing this gene/protein

cell envelope stress proteins (controlled by SigM, W, X, Y), membrane proteins, poorly characterized/ putative enzymes

The protein

Basic information/ Evolution

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

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization: cell membrane (according to Swiss-Prot)

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • 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

Min Cao, John D Helmann
The Bacillus subtilis extracytoplasmic-function sigmaX factor regulates modification of the cell envelope and resistance to cationic antimicrobial peptides.
J Bacteriol: 2004, 186(4);1136-46
[PubMed:14762009] [WorldCat.org] [DOI] (P p)