Difference between revisions of "DhbC"
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− | <pubmed>8224884,11112781 ,11790741,12354229,17218307, 8921902 8550523 | + | <pubmed>8224884,11112781 ,11790741,12354229,17218307, 8921902 8550523 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 14:56, 16 April 2011
- Description: isochorismate synthase
Gene name | dhbC |
Synonyms | |
Essential | no |
Product | isochorismate synthase |
Function | biosynthesis of the siderophore bacillibactin |
MW, pI | 43 kDa, 5.168 |
Gene length, protein length | 1194 bp, 398 aa |
Immediate neighbours | dhbE, dhbA |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
Categories containing this gene/protein
acquisition of iron, iron metabolism, phosphoproteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU31990
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Chorismate = isochorismate (according to Swiss-Prot)
- Protein family: isochorismate synthase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification: phosphorylation on Ser-271 PubMed
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure: 3OS6, (from B. anthracis, 56% identity, 70% similarity)
- UniProt: P45744
- KEGG entry: [3]
- E.C. number: 5.4.4.2
Additional information
Expression and regulation
- 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
Additional publications: PubMed
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)
R Adams, W Schumann
Cloning and mapping of the Bacillus subtilis locus homologous to Escherichia coli ent genes.
Gene: 1993, 133(1);119-21
[PubMed:8224884]
[WorldCat.org]
[DOI]
(P p)