Difference between revisions of "DhbB"

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* '''Operon:''' ''[[dhbA]]-[[dhbC]]-[[dhbE]]-[[dhbB]]-[[dhbF]]'' {{PubMed|8921902}}
 
* '''Operon:''' ''[[dhbA]]-[[dhbC]]-[[dhbE]]-[[dhbB]]-[[dhbF]]'' {{PubMed|8921902}}
  
* '''[[Sigma factor]]:''' [[SigA]] {{PubMed|8550523}}
+
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=dhbB_3287675_3288613_-1 dhbB] {{PubMed|22383849}}
 +
 
 +
* '''Sigma factor:''' [[SigA]] {{PubMed|8550523}}
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  

Revision as of 16:32, 16 April 2012

  • Description: isochorismatase

Gene name dhbB
Synonyms
Essential no
Product isochorismatase
Function biosynthesis of the siderophore bacillibactin
MW, pI 34 kDa, 4.429
Gene length, protein length 936 bp, 312 aa
Immediate neighbours dhbF, dhbE
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
DhbB context.gif
This image was kindly provided by SubtiList



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: BSU31970

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Isochorismate + H2O = 2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate (according to Swiss-Prot)
  • Protein family: isochorismatase 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:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:
    • the amount of the mRNA is substantially decreased upon depletion of RNase Y PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Additional publications: PubMed

Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J  
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y. 
Mol Microbiol. 2011 81(6): 1459-1473. 
PubMed:21815947

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)