DhbE

• 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
MW, pI	59 kDa, 5.684
Gene length, protein length	1617 bp, 539 aa
Immediate neighbours	dhbB, dhbC
Sequences	Protein DNA Advanced_DNA
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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

• UniProt: P40871

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: dhbA-dhbC-dhbE-dhbB-dhbF PubMed

• Expression browser: dhbE PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • induced by iron starvation (Fur) PubMed

• Regulatory mechanism:
  • Fur: transcription repression PubMed
  • AbrB: transcription repression PubMed

• 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

Mohamed Marahiel, Marburg University, Germany homepage

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)

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)