Difference between revisions of "DhbF"

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= Categories containing this gene/protein =
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{{SubtiWiki category|[[acquisition of iron]]}},
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{{SubtiWiki category|[[iron metabolism]]}},
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{{SubtiWiki category|[[membrane proteins]]}},
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{{SubtiWiki category|[[phosphoproteins]]}}
 
=The protein=
 
=The protein=
  

Revision as of 16:18, 30 November 2010

  • Description: involved in 2,3-dihydroxybenzoate biosynthesis

Gene name dhbF
Synonyms
Essential no
Product unknown
Function biosynthesis of the siderophore bacillibactin
MW, pI 263 kDa, 4.737
Gene length, protein length 7134 bp, 2378 aa
Immediate neighbours yukJ, dhbB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
DhbF context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU31960

Phenotypes of a mutant

Database entries

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

Additional information

Categories containing this gene/protein

acquisition of iron, iron metabolism, membrane proteins, phosphoproteins

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: ATP-dependent AMP-binding enzyme family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylation on Ser-988 AND Ser-996 PubMed
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization: membrane PubMed

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

Onuma Chumsakul, Hiroki Takahashi, Taku Oshima, Takahiro Hishimoto, Shigehiko Kanaya, Naotake Ogasawara, Shu Ishikawa
Genome-wide binding profiles of the Bacillus subtilis transition state regulator AbrB and its homolog Abh reveals their interactive role in transcriptional regulation.
Nucleic Acids Res: 2011, 39(2);414-28
[PubMed:20817675] [WorldCat.org] [DOI] (I p)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)

Noel Baichoo, Tao Wang, Rick Ye, John D Helmann
Global analysis of the Bacillus subtilis Fur regulon and the iron starvation stimulon.
Mol Microbiol: 2002, 45(6);1613-29
[PubMed:12354229] [WorldCat.org] [DOI] (P p)

Tamara Hoffmann, Alexandra Schütz, Margot Brosius, Andrea Völker, Uwe Völker, Erhard Bremer
High-salinity-induced iron limitation in Bacillus subtilis.
J Bacteriol: 2002, 184(3);718-27
[PubMed:11790741] [WorldCat.org] [DOI] (P p)

J J May, T M Wendrich, M A Marahiel
The dhb operon of Bacillus subtilis encodes the biosynthetic template for the catecholic siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin.
J Biol Chem: 2001, 276(10);7209-17
[PubMed:11112781] [WorldCat.org] [DOI] (P p)

B M Rowland, T H Grossman, M S Osburne, H W Taber
Sequence and genetic organization of a Bacillus subtilis operon encoding 2,3-dihydroxybenzoate biosynthetic enzymes.
Gene: 1996, 178(1-2);119-23
[PubMed:8921902] [WorldCat.org] [DOI] (P p)

B M Rowland, H W Taber
Duplicate isochorismate synthase genes of Bacillus subtilis: regulation and involvement in the biosyntheses of menaquinone and 2,3-dihydroxybenzoate.
J Bacteriol: 1996, 178(3);854-61
[PubMed:8550523] [WorldCat.org] [DOI] (P p)