PhoP

• Description: two-component response regulator, regulation of phosphate metabolism
  
  

Gene name	phoP
Synonyms
Essential	no
Product	two-component response regulator
Function	regulation of phosphate metabolism (phoA, phoB, phoD, resABCDE, tagA-tagB, tagDEF, tuaA-H)
Interactions involving this protein in SubtInteract: PhoP
Metabolic function and regulation of this protein in SubtiPathways: Folate, Protein secretion
MW, pI	27 kDa, 5.068
Gene length, protein length	720 bp, 240 aa
Immediate neighbours	phoR, mdh
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, transcription factors and their control, regulators of core metabolism, sporulation proteins, general stress proteins (controlled by SigB), membrane proteins, phosphoproteins

This gene is a member of the following regulons

CcpA regulon, PhoP regulon, SigB regulon, SigE regulon

The gene

Basic information

• Locus tag: BSU29110

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification: phosphorylation by PhoR under conditions of phosphate limitation (stimulates DNA-binding activity)

• Cofactor(s):

• Effectors of protein activity: phosphorylation stimulates DNA-binding activity

• Interactions: PhoP-PhoP, PhoP-PhoR

• Localization: cell membrane (according to Swiss-Prot)

Database entries

• Structure: 1MVO (receiver domain)

• UniProt: P13792

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: phoP-phoR PubMed

• Sigma factor: SigA PubMed, SigB PubMed, SigE PubMed

• Regulation:
  • carbon catabolite repression (CcpA) PubMed
  • expressed under conditions of phosphate limitation (PhoP) PubMed
  • expressed in post-exponential phase (ScoC) PubMed

• Regulatory mechanism:
  • CcpA: transcription repression PubMed
  • PhoP: transcription activation PubMed
  • ScoC: transcription repression PubMed

• 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

References

Eric Botella, Sebastian Hübner, Karsten Hokamp, Annette Hansen, Paola Bisicchia, David Noone, Leagh Powell, Letal I Salzberg, Kevin M Devine
Cell envelope gene expression in phosphate-limited Bacillus subtilis cells.
Microbiology (Reading): 2011, 157(Pt 9);2470-2484
[PubMed:21636651] [WorldCat.org] [DOI] (I p)

Bindiya Kaushal, Salbi Paul, F Marion Hulett
Direct regulation of Bacillus subtilis phoPR transcription by transition state regulator ScoC.
J Bacteriol: 2010, 192(12);3103-13
[PubMed:20382764] [WorldCat.org] [DOI] (I p)

Inga Jende, Kottayil I Varughese, Kevin M Devine
Amino acid identity at one position within the alpha1 helix of both the histidine kinase and the response regulator of the WalRK and PhoPR two-component systems plays a crucial role in the specificity of phosphotransfer.
Microbiology (Reading): 2010, 156(Pt 6);1848-1859
[PubMed:20167622] [WorldCat.org] [DOI] (I p)

Salbi Paul, Stephanie Birkey, Wei Liu, F Marion Hulett
Autoinduction of Bacillus subtilis phoPR operon transcription results from enhanced transcription from EsigmaA- and EsigmaE-responsive promoters by phosphorylated PhoP.
J Bacteriol: 2004, 186(13);4262-75
[PubMed:15205429] [WorldCat.org] [DOI] (P p)

Zoltán Prágai, Nicholas E E Allenby, Nicola O'Connor, Sarah Dubrac, Georges Rapoport, Tarek Msadek, Colin R Harwood
Transcriptional regulation of the phoPR operon in Bacillus subtilis.
J Bacteriol: 2004, 186(4);1182-90
[PubMed:14762014] [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)

Yinghua Chen, Catherine Birck, Jean-Pierre Samama, F Marion Hulett
Residue R113 is essential for PhoP dimerization and function: a residue buried in the asymmetric PhoP dimer interface determined in the PhoPN three-dimensional crystal structure.
J Bacteriol: 2003, 185(1);262-73
[PubMed:12486063] [WorldCat.org] [DOI] (P p)

Y Qi, F M Hulett
Role of Pho-P in transcriptional regulation of genes involved in cell wall anionic polymer biosynthesis in Bacillus subtilis.
J Bacteriol: 1998, 180(15);4007-10
[PubMed:9683503] [WorldCat.org] [DOI] (P p)

Y Qi, F M Hulett
PhoP-P and RNA polymerase sigmaA holoenzyme are sufficient for transcription of Pho regulon promoters in Bacillus subtilis: PhoP-P activator sites within the coding region stimulate transcription in vitro.
Mol Microbiol: 1998, 28(6);1187-97
[PubMed:9680208] [WorldCat.org] [DOI] (P p)

W Liu, S Eder, F M Hulett
Analysis of Bacillus subtilis tagAB and tagDEF expression during phosphate starvation identifies a repressor role for PhoP-P.
J Bacteriol: 1998, 180(3);753-8
[PubMed:9457886] [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)