Difference between revisions of "PhoD"

From SubtiWiki
Jump to: navigation, search
Line 80: Line 80:
 
* '''Kinetic information:'''
 
* '''Kinetic information:'''
  
* '''Domains:'''  
+
* '''[[Domains]]:'''  
  
 
* '''Modification:'''
 
* '''Modification:'''
  
* '''Cofactor(s):'''
+
* '''[[Cofactors]]:'''
  
 
* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
Line 144: Line 144:
  
 
=References=
 
=References=
Additional publications: {{PubMed|22960285}}
+
== Reviews ==
<pubmed>8760916,10913081,12867413,10094677,12218047,10556724,19180538,10094677, 18957862, 19383693, 19395490 22383849 23180473</pubmed>
+
<pubmed> 24140208 </pubmed>
 +
== Original publications ==
 +
<pubmed>8760916,10913081,12867413,10094677,12218047,10556724,19180538,10094677, 18957862, 19383693, 19395490 22960285 22383849 23180473</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 14:11, 6 December 2013

  • 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 yczK, tatAD
Sequences Protein DNA DNA_with_flanks
Genetic context
PhoD context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PhoD expression.png















Categories containing this gene/protein

phosphate metabolism

This gene is a member of the following regulons

PhoP regulon

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:
  • Modification:
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • expressed under conditions of phosphate limitation (PhoP) PubMed
  • Regulatory mechanism:
  • 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

Reviews

Original publications

Carmine G Monteferrante, Calum MacKichan, Elodie Marchadier, Maria-Victoria Prejean, Rut Carballido-López, Jan Maarten van Dijl
Mapping the twin-arginine protein translocation network of Bacillus subtilis.
Proteomics: 2013, 13(5);800-11
[PubMed:23180473] [WorldCat.org] [DOI] (I p)

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)

Pierre Nicolas, Ulrike Mäder, Etienne Dervyn, Tatiana Rochat, Aurélie Leduc, Nathalie Pigeonneau, Elena Bidnenko, Elodie Marchadier, Mark Hoebeke, Stéphane Aymerich, Dörte Becher, Paola Bisicchia, Eric Botella, Olivier Delumeau, Geoff Doherty, Emma L Denham, Mark J Fogg, Vincent Fromion, Anne Goelzer, Annette Hansen, Elisabeth Härtig, Colin R Harwood, Georg Homuth, Hanne Jarmer, Matthieu Jules, Edda Klipp, Ludovic Le Chat, François Lecointe, Peter Lewis, Wolfram Liebermeister, Anika March, Ruben A T Mars, Priyanka Nannapaneni, David Noone, Susanne Pohl, Bernd Rinn, Frank Rügheimer, Praveen K Sappa, Franck Samson, Marc Schaffer, Benno Schwikowski, Leif Steil, Jörg Stülke, Thomas Wiegert, Kevin M Devine, Anthony J Wilkinson, Jan Maarten van Dijl, Michael Hecker, Uwe Völker, Philippe Bessières, Philippe Noirot
Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis.
Science: 2012, 335(6072);1103-6
[PubMed:22383849] [WorldCat.org] [DOI] (I 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)