Difference between revisions of "YfiT"

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= [[Categories]] containing this gene/protein =
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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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=The gene=
 
=The gene=
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= Categories containing this gene/protein =
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{{SubtiWiki category|[[poorly characterized/ putative enzymes]]}}
 
 
=The protein=
 
=The protein=
  

Revision as of 17:48, 8 December 2010

  • Description: probable metal-dependent hydrolase

Gene name yfiT
Synonyms
Essential no
Product unknown
Function unknown
MW, pI 20 kDa, 6.612
Gene length, protein length 534 bp, 178 aa
Immediate neighbours yfiS, yfiU
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YfiT context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

poorly characterized/ putative enzymes

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU08390

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

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

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Effectors of protein activity:
  • Interactions: homodimer PubMed
  • Localization: cytoplasm (according to Swiss-Prot)

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Operon: yfiT (according to DBTBS)
  • 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

Shyamala S Rajan, Xiaojing Yang, Ludmilla Shuvalova, Frank Collart, Wayne F Anderson
YfiT from Bacillus subtilis is a probable metal-dependent hydrolase with an unusual four-helix bundle topology.
Biochemistry: 2004, 43(49);15472-9
[PubMed:15581359] [WorldCat.org] [DOI] (P p)