RapA

• Description: response regulator aspartate phosphatase, dephosphorylates Spo0F-P, control of the phosphorelay
  
  

Gene name	rapA
Synonyms	gsiAA, spo0L
Essential	no
Product	response regulator aspartate phosphatase
Function	control of sporulation initiation
Gene expression levels in SubtiExpress: rapA
Interactions involving this protein in SubtInteract: RapA
Function and regulation of this protein in SubtiPathways: rapA
MW, pI	44 kDa, 4.848
Gene length, protein length	1134 bp, 378 aa
Immediate neighbours	yjoB, phrA
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

protein modification, transcription factors and their control, phosphorelay, quorum sensing

This gene is a member of the following regulons

CodY regulon, ComA regulon, Spo0A regulon

The gene

Basic information

• Locus tag: BSU12430

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

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

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:
  • modular organization comprising an amino terminal alpha-helical domain connected to a domain formed by six tetratricopeptide (TPR) repeats PubMed

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • RapA (central TPR3-5 repeats) -PhrA PubMed
  • RapA (N-terminal 60 amino acids) -Spo0F PubMed

• Localization:

Database entries

• Structure:

• UniProt: Q00828

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: rapA-phrA PubMed

• Expression browser: rapA 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
  • expressed at high cell density (ComA) PubMed

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

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Boris R Belitsky, Abraham L Sonenshein
Genome-wide identification of Bacillus subtilis CodY-binding sites at single-nucleotide resolution.
Proc Natl Acad Sci U S A: 2013, 110(17);7026-31
[PubMed:23569278] [WorldCat.org] [DOI] (I p)

Alejandra R Diaz, Leighton J Core, Min Jiang, Michela Morelli, Christina H Chiang, Hendrik Szurmant, Marta Perego
Bacillus subtilis RapA phosphatase domain interaction with its substrate, phosphorylated Spo0F, and its inhibitor, the PhrA peptide.
J Bacteriol: 2012, 194(6);1378-88
[PubMed:22267516] [WorldCat.org] [DOI] (I p)

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)

Natalia Comella, Alan D Grossman
Conservation of genes and processes controlled by the quorum response in bacteria: characterization of genes controlled by the quorum-sensing transcription factor ComA in Bacillus subtilis.
Mol Microbiol: 2005, 57(4);1159-74
[PubMed:16091051] [WorldCat.org] [DOI] (P 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)

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135] [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)