Difference between revisions of "DhbE"

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* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1MDB 1MDB] (complex with DHB-adenylate),  [http://www.rcsb.org/pdb/explore.do?structureId=1MDF 1MDF]
 
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1MDB 1MDB] (complex with DHB-adenylate),  [http://www.rcsb.org/pdb/explore.do?structureId=1MDF 1MDF]
  
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P40871 P40871]
+
* '''UniProt:''' [http://www.uniprot.org/uniprot/P40871 P40871]
  
 
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU31980]
 
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU31980]

Revision as of 14:22, 20 July 2009

  • Description: 2,3-dihydroxybenzoate-AMP ligase (enterobactin synthetase component E)

Gene name dhbE
Synonyms entE
Essential no
Product 2,3-dihydroxybenzoate-AMP ligase (enterobactin synthetase component E)
Function siderophore biosynthesis
MW, pI 59 kDa, 5.684
Gene length, protein length 1617 bp, 539 aa
Immediate neighbours dhbB, dhbC
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
DhbE context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU31980

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: ATP-dependent AMP-binding enzyme 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: cytoplasm (according to Swiss-Prot)

Database entries

  • Structure: 1MDB (complex with DHB-adenylate), 1MDF
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Regulation:
    • repressed unless the cells enter an iron starvation (Fur) PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Mohamed Marahiel, Marburg University, Germany homepage

Your additional remarks

References

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)

Jurgen J May, Nadine Kessler, Mohamed A Marahiel, Milton T Stubbs
Crystal structure of DhbE, an archetype for aryl acid activating domains of modular nonribosomal peptide synthetases.
Proc Natl Acad Sci U S A: 2002, 99(19);12120-5
[PubMed:12221282] [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)