Difference between revisions of "DhbC"
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* '''Additional information:''' | * '''Additional information:''' | ||
** the amount of the mRNA is substantially decreased upon depletion of [[Rny|RNase Y]] {{PubMed|21815947}} | ** the amount of the mRNA is substantially decreased upon depletion of [[Rny|RNase Y]] {{PubMed|21815947}} | ||
+ | ** number of protein molecules per cell (minimal medium with glucose and ammonium): 9037 {{PubMed|24696501}} | ||
+ | ** number of protein molecules per cell (complex medium with amino acids, without glucose): 3893 {{PubMed|24696501}} | ||
=Biological materials = | =Biological materials = |
Revision as of 09:24, 17 April 2014
- Description: isochorismate synthase
Gene name | dhbC |
Synonyms | |
Essential | no |
Product | isochorismate synthase |
Function | biosynthesis of the siderophore bacillibactin |
Gene expression levels in SubtiExpress: dhbC | |
Metabolic function and regulation of this protein in SubtiPathways: DhbC | |
MW, pI | 43 kDa, 5.168 |
Gene length, protein length | 1194 bp, 398 aa |
Immediate neighbours | dhbE, dhbA |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
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
- BsubCyc: BSU31990
- 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:
Database entries
- BsubCyc: BSU31990
- 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
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)
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)