Difference between revisions of "PhoD"
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[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 17:33, 11 September 2012
- Description: phosphodiesterase/alkaline phosphatase
Gene name | phoD |
Synonyms | ycbS |
Essential | no |
Product | phosphodiesterase/alkaline phosphatase |
Function | aquisition of phosphate upon phosphoate starvation |
Gene expression levels in SubtiExpress: phoD | |
Interactions involving this protein in SubtInteract: PhoD | |
Metabolic function and regulation of this protein in SubtiPathways: Protein secretion | |
MW, pI | 62 kDa, 8.394 |
Gene length, protein length | 1668 bp, 556 aa |
Immediate neighbours | ycbR, tatAD |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU02620
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:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: extracellular (signal peptide) PubMed, secreted by the TatAD-TatCD complex PubMed
Database entries
- Structure: 2YEQ
- UniProt: P42251
- 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
Oscar Kuipers, University of Groningen, The Netherlands Homepage
Your additional remarks
References
Marco J Klein, Stephan L Grage, Claudia Muhle-Goll, Jochen Bürck, Sergii Afonin, Anne S Ulrich
Structure analysis of the membrane-bound PhoD signal peptide of the Tat translocase shows an N-terminal amphiphilic helix.
Biochim Biophys Acta: 2012, 1818(12);3025-31
[PubMed:22960285]
[WorldCat.org]
[DOI]
(P p)
Anja N J A Ridder, Esther J de Jong, Jan D H Jongbloed, Oscar P Kuipers
Subcellular localization of TatAd of Bacillus subtilis depends on the presence of TatCd or TatCy.
J Bacteriol: 2009, 191(13);4410-8
[PubMed:19395490]
[WorldCat.org]
[DOI]
(I p)
Robyn T Eijlander, Magdalena A Kolbusz, Erwin M Berendsen, Oscar P Kuipers
Effects of altered TatC proteins on protein secretion efficiency via the twin-arginine translocation pathway of Bacillus subtilis.
Microbiology (Reading): 2009, 155(Pt 6);1776-1785
[PubMed:19383693]
[WorldCat.org]
[DOI]
(P p)
Thijs R H M Kouwen, René van der Ploeg, Haike Antelmann, Michael Hecker, Georg Homuth, Ulrike Mäder, Jan Maarten van Dijl
Overflow of a hyper-produced secretory protein from the Bacillus Sec pathway into the Tat pathway for protein secretion as revealed by proteogenomics.
Proteomics: 2009, 9(4);1018-32
[PubMed:19180538]
[WorldCat.org]
[DOI]
(I p)
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)
Ovidiu I Pop, Martin Westermann, Rudolf Volkmer-Engert, Daniela Schulz, Cornelius Lemke, Sandra Schreiber, Roman Gerlach, Reinhard Wetzker, Jörg P Müller
Sequence-specific binding of prePhoD to soluble TatAd indicates protein-mediated targeting of the Tat export in Bacillus subtilis.
J Biol Chem: 2003, 278(40);38428-36
[PubMed:12867413]
[WorldCat.org]
[DOI]
(P p)
Jan D H Jongbloed, Haike Antelmann, Michael Hecker, Reindert Nijland, Sierd Bron, Ulla Airaksinen, Frens Pries, Wim J Quax, Jan Maarten van Dijl, Peter G Braun
Selective contribution of the twin-arginine translocation pathway to protein secretion in Bacillus subtilis.
J Biol Chem: 2002, 277(46);44068-78
[PubMed:12218047]
[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)
J P Müller, M Wagner
Localisation of the cell wall-associated phosphodiesterase PhoD of Bacillus subtilis.
FEMS Microbiol Lett: 1999, 180(2);287-96
[PubMed:10556724]
[WorldCat.org]
[DOI]
(P p)
S Eder, W Liu, F M Hulett
Mutational analysis of the phoD promoter in Bacillus subtilis: implications for PhoP binding and promoter activation of Pho regulon promoters.
J Bacteriol: 1999, 181(7);2017-25
[PubMed:10094677]
[WorldCat.org]
[DOI]
(P p)
S Eder, L Shi, K Jensen, K Yamane, F M Hulett
A Bacillus subtilis secreted phosphodiesterase/alkaline phosphatase is the product of a Pho regulon gene, phoD.
Microbiology (Reading): 1996, 142 ( Pt 8);2041-7
[PubMed:8760916]
[WorldCat.org]
[DOI]
(P p)