PhoB

• Description: alkaline phosphatase III
  
  

Gene name	phoB
Synonyms	phoAIII
Essential	no
Product	alkaline phosphatase III
Function	aquisition of phosphate upon phosphoate starvation
Gene expression levels in SubtiExpress: phoB
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
Sequences	Protein DNA Advanced_DNA
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

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:
  • 1A767 ( phoB::cat), PubMed, available at BGSC

• 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)