Difference between revisions of "DhbE"

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** number of protein molecules per cell (minimal medium with glucose and ammonium): 4899 {{PubMed|24696501}}
 
** number of protein molecules per cell (minimal medium with glucose and ammonium): 4899 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 1656 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 1656 {{PubMed|24696501}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 10561 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 4162 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 3499 {{PubMed|21395229}}
  
 
=Biological materials =
 
=Biological materials =
 
 
* '''Mutant:'''
 
* '''Mutant:'''
  

Revision as of 14:05, 17 April 2014

  • 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 biosynthesis of the siderophore bacillibactin
Gene expression levels in SubtiExpress: dhbE
Metabolic function and regulation of this protein in SubtiPathways:
DhbE
MW, pI 59 kDa, 5.684
Gene length, protein length 1617 bp, 539 aa
Immediate neighbours dhbB, dhbC
Sequences Protein DNA DNA_with_flanks
Genetic context
DhbE context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
DhbE expression.png















Categories containing this gene/protein

acquisition of iron, iron metabolism

This gene is a member of the following regulons

AbrB regulon, Fur regulon

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:

Database entries

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

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:
    • the amount of the mRNA is substantially decreased upon depletion of RNase Y PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 4899 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 1656 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 10561 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 4162 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 3499 PubMed

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

Martin Lehnik-Habrink, Marc Schaffer, Ulrike Mäder, Christine Diethmaier, Christina Herzberg, Jörg Stülke
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y.
Mol Microbiol: 2011, 81(6);1459-73
[PubMed:21815947] [WorldCat.org] [DOI] (I p)

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)

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)

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)