Difference between revisions of "PhoA"

From SubtiWiki
Jump to: navigation, search
Line 82: Line 82:
 
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P19406 P19406]
 
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P19406 P19406]
  
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU09410]
+
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU09410]
  
 
* '''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 phoA
Synonyms phoAIV
Essential no
Product alkaline phosphatase A
Function aquisition of phosphate upon phosphoate starvation
MW, pI 50 kDa, 9.926
Gene length, protein length 1383 bp, 461 aa
Immediate neighbours spoVR, lytE
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
PhoA context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU09410

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): PhoB

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization: extracellular (signal peptide) PubMed

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Operon:
  • 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)

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, Y Qi, F M Hulett
Sites internal to the coding regions of phoA and pstS bind PhoP and are required for full promoter activity.
Mol Microbiol: 1998, 28(1);119-30
[PubMed:9593301] [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)