Difference between revisions of "PhoB"
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* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P19405 P19405] | * '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P19405 P19405] | ||
− | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu | + | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU05740] |
* '''E.C. number:''' [http://www.expasy.org/enzyme/3.1.3.1 3.1.3.1] | * '''E.C. number:''' [http://www.expasy.org/enzyme/3.1.3.1 3.1.3.1] |
Revision as of 03:42, 25 June 2009
- Description: alkaline phosphatase A
Gene name | phoB |
Synonyms | phoAIII |
Essential | no |
Product | alkaline phosphatase A |
Function | aquisition of phosphate upon phosphoate starvation |
Metabolic function and regulation of this protein in SubtiPathways: Folate | |
MW, pI | 50 kDa, 5.895 |
Gene length, protein length | 1386 bp, 462 aa |
Immediate neighbours | ydhF, ydhG |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU05740
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: A phosphate monoester + H2O = an alcohol + phosphate (according to Swiss-Prot)
- Protein family: alkaline phosphatase family (according to Swiss-Prot)
- Paralogous protein(s): PhoA
Extended information on the protein
- Kinetic information:
- Domains:
- Modification: phosphorylated on ser/ thr/ tyr PubMed
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: extracellular (signal peptide) PubMed
Database entries
- Structure:
- Swiss prot entry: P19405
- KEGG entry: [3]
- E.C. number: 3.1.3.1
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
Marion Hulett, University of Illinois at Chicago, USA Homepage
Your additional remarks
References
Birgit Voigt, Haike Antelmann, Dirk Albrecht, Armin Ehrenreich, Karl-Heinz Maurer, Stefan Evers, Gerhard Gottschalk, Jan Maarten van Dijl, Thomas Schweder, Michael Hecker
Cell physiology and protein secretion of Bacillus licheniformis compared to Bacillus subtilis.
J Mol Microbiol Biotechnol: 2009, 16(1-2);53-68
[PubMed:18957862]
[WorldCat.org]
[DOI]
(I p)
Alain Lévine, Françoise Vannier, Cédric Absalon, Lauriane Kuhn, Peter Jackson, Elaine Scrivener, Valérie Labas, Joëlle Vinh, Patrick Courtney, Jérôme Garin, Simone J Séror
Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes.
Proteomics: 2006, 6(7);2157-73
[PubMed:16493705]
[WorldCat.org]
[DOI]
(P p)
Wael R Abdel-Fattah, Yinghua Chen, Amr Eldakak, F Marion Hulett
Bacillus subtilis phosphorylated PhoP: direct activation of the E(sigma)A- and repression of the E(sigma)E-responsive phoB-PS+V promoters during pho response.
J Bacteriol: 2005, 187(15);5166-78
[PubMed:16030210]
[WorldCat.org]
[DOI]
(P p)
H Antelmann, C Scharf, M Hecker
Phosphate starvation-inducible proteins of Bacillus subtilis: proteomics and transcriptional analysis.
J Bacteriol: 2000, 182(16);4478-90
[PubMed:10913081]
[WorldCat.org]
[DOI]
(P p)
W Liu, F M Hulett
Bacillus subtilis PhoP binds to the phoB tandem promoter exclusively within the phosphate starvation-inducible promoter.
J Bacteriol: 1997, 179(20);6302-10
[PubMed:9335276]
[WorldCat.org]
[DOI]
(P p)
S M Birkey, G Sun, P J Piggot, F M Hulett
A pho regulon promoter induced under sporulation conditions.
Gene: 1994, 147(1);95-100
[PubMed:8088554]
[WorldCat.org]
[DOI]
(P p)
F M Hulett, J Lee, L Shi, G Sun, R Chesnut, E Sharkova, M F Duggan, N Kapp
Sequential action of two-component genetic switches regulates the PHO regulon in Bacillus subtilis.
J Bacteriol: 1994, 176(5);1348-58
[PubMed:8113174]
[WorldCat.org]
[DOI]
(P p)