PhrA

• Description: phosphatase (response regulator aspartate phosphatase RapA) inhibitor, control of the phosphorelay
  
  

Gene name	phrA
Synonyms	gsiAB
Essential	no
Product	phosphatase (RapA) inhibitor
Function	control of sporulation initiation
MW, pI	4 kDa, 10.229
Gene length, protein length	132 bp, 44 aa
Immediate neighbours	rapA, yjpA
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU12440

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: phr family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions: RapA-PhrA

• Localization:

Database entries

• Structure:

• UniProt: Q00829

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: rapA-phrA PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • repressed by glucose (4.2-fold) (CcpA) PubMed
  • repressed by casamino acids PubMed
  • repressed under conditions that trigger sporulation (Spo0A) PubMed
  • repressed during growth in the presence of branched chain amino acids (CodY) PubMed

• Regulatory mechanism:
  • CcpA: transcription repression
  • Spo0A: transcription repression PubMed
  • CodY: transcription repression PubMed
  • ComA: transcription activation PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Ilka B Bischofs, Joshua A Hug, Aiwen W Liu, Denise M Wolf, Adam P Arkin
Complexity in bacterial cell-cell communication: quorum signal integration and subpopulation signaling in the Bacillus subtilis phosphorelay.
Proc Natl Acad Sci U S A: 2009, 106(16);6459-64
[PubMed:19380751] [WorldCat.org] [DOI] (I p)

Virginie Molle, Masaya Fujita, Shane T Jensen, Patrick Eichenberger, José E González-Pastor, Jun S Liu, Richard Losick
The Spo0A regulon of Bacillus subtilis.
Mol Microbiol: 2003, 50(5);1683-701
[PubMed:14651647] [WorldCat.org] [DOI] (P p)

Virginie Molle, Yoshiko Nakaura, Robert P Shivers, Hirotake Yamaguchi, Richard Losick, Yasutaro Fujita, Abraham L Sonenshein
Additional targets of the Bacillus subtilis global regulator CodY identified by chromatin immunoprecipitation and genome-wide transcript analysis.
J Bacteriol: 2003, 185(6);1911-22
[PubMed:12618455] [WorldCat.org] [DOI] (P p)

Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability.
J Bacteriol: 2002, 184(15);4288-95
[PubMed:12107147] [WorldCat.org] [DOI] (P p)

Shu Ishikawa, Leighton Core, Marta Perego
Biochemical characterization of aspartyl phosphate phosphatase interaction with a phosphorylated response regulator and its inhibition by a pentapeptide.
J Biol Chem: 2002, 277(23);20483-9
[PubMed:11923303] [WorldCat.org] [DOI] (P p)

M Perego, P Glaser, J A Hoch
Aspartyl-phosphate phosphatases deactivate the response regulator components of the sporulation signal transduction system in Bacillus subtilis.
Mol Microbiol: 1996, 19(6);1151-7
[PubMed:8730857] [WorldCat.org] [DOI] (P p)

M Perego, J A Hoch
Cell-cell communication regulates the effects of protein aspartate phosphatases on the phosphorelay controlling development in Bacillus subtilis.
Proc Natl Acad Sci U S A: 1996, 93(4);1549-53
[PubMed:8643670] [WorldCat.org] [DOI] (P p)

J P Mueller, G Bukusoglu, A L Sonenshein
Transcriptional regulation of Bacillus subtilis glucose starvation-inducible genes: control of gsiA by the ComP-ComA signal transduction system.
J Bacteriol: 1992, 174(13);4361-73
[PubMed:1378051] [WorldCat.org] [DOI] (P p)