Difference between revisions of "PhoB"

From SubtiWiki
Jump to: navigation, search
Line 33: Line 33:
 
__TOC__
 
__TOC__
  
<br/><br/>
+
<br/><br/><br/><br/><br/><br/>
  
 
=The gene=
 
=The gene=

Revision as of 15:28, 22 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
PhoB context.gif
This image was kindly provided by SubtiList







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:
  • 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

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)