PhoB

• Description: alkaline phosphatase III
  
  

Gene name	phoB
Synonyms	phoAIII
Essential	no
Product	alkaline phosphatase III
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, fra
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

phosphate metabolism, sporulation proteins

This gene is a member of the following regulons

PhoP regulon, SigE regulon

The gene

Basic information

• Locus tag: BSU05740

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• UniProt: P19405

• KEGG entry: [3]

• E.C. number: 3.1.3.1

Expression and regulation

• Operon: phoB-ydhF PubMed

• Expression browser: phoB PubMed

• Sigma factor: SigA, SigE PubMed

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

• Regulatory mechanism:
  • PhoP: transcription activation PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)

Soo-Keun Choi, Milton H Saier
Regulation of pho regulon gene expression by the carbon control protein A, CcpA, in Bacillus subtilis.
J Mol Microbiol Biotechnol: 2005, 10(1);40-50
[PubMed:16491025] [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)