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)

Amr Eldakak, F Marion Hulett
Cys303 in the histidine kinase PhoR is crucial for the phosphotransfer reaction in the PhoPR two-component system in Bacillus subtilis.
J Bacteriol: 2007, 189(2);410-21
[PubMed:17085571] [WorldCat.org] [DOI] (P p)

Ankita Puri-Taneja, Salbi Paul, Yinghua Chen, F Marion Hulett
CcpA causes repression of the phoPR promoter through a novel transcription start site, P(A6).
J Bacteriol: 2006, 188(4);1266-78
[PubMed:16452408] [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)

Matthew Schau, Amr Eldakak, F Marion Hulett
Terminal oxidases are essential to bypass the requirement for ResD for full Pho induction in Bacillus subtilis.
J Bacteriol: 2004, 186(24);8424-32
[PubMed:15576792] [WorldCat.org] [DOI] (P 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)

Yinghua Chen, Wael R Abdel-Fattah, F Marion Hulett
Residues required for Bacillus subtilis PhoP DNA binding or RNA polymerase interaction: alanine scanning of PhoP effector domain transactivation loop and alpha helix 3.
J Bacteriol: 2004, 186(5);1493-502
[PubMed:14973033] [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)

Catherine Birck, Yinghua Chen, F Marion Hulett, Jean-Pierre Samama
The crystal structure of the phosphorylation domain in PhoP reveals a functional tandem association mediated by an asymmetric interface.
J Bacteriol: 2003, 185(1);254-61
[PubMed:12486062] [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)

L Shi, W Liu, F M Hulett
Decay of activated Bacillus subtilis pho response regulator, PhoP approximately P, involves the PhoR approximately P intermediate.
Biochemistry: 1999, 38(31);10119-25
[PubMed:10433720] [WorldCat.org] [DOI] (P p)

S Eder, W Liu, F M Hulett
Mutational analysis of the phoD promoter in Bacillus subtilis: implications for PhoP binding and promoter activation of Pho regulon promoters.
J Bacteriol: 1999, 181(7);2017-25
[PubMed:10094677] [WorldCat.org] [DOI] (P p)

C Fabret, V A Feher, J A Hoch
Two-component signal transduction in Bacillus subtilis: how one organism sees its world.
J Bacteriol: 1999, 181(7);1975-83
[PubMed:10094672] [WorldCat.org] [DOI] (P p)

S M Birkey, W Liu, X Zhang, M F Duggan, F M Hulett
Pho signal transduction network reveals direct transcriptional regulation of one two-component system by another two-component regulator: Bacillus subtilis PhoP directly regulates production of ResD.
Mol Microbiol: 1998, 30(5);943-53
[PubMed:9988472] [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)

Wei Liu, F Marion Hulett
Comparison of PhoP binding to the tuaA promoter with PhoP binding to other Pho-regulon promoters establishes a Bacillus subtilis Pho core binding site.
Microbiology (Reading): 1998, 144 ( Pt 5);1443-1450
[PubMed:9611818] [WorldCat.org] [DOI] (P p)

W Liu, Y Qi, F M Hulett
Sites internal to the coding regions of phoA and pstS bind PhoP and are required for full promoter activity.
Mol Microbiol: 1998, 28(1);119-30
[PubMed:9593301] [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)

Y Qi, Y Kobayashi, F M Hulett
The pst operon of Bacillus subtilis has a phosphate-regulated promoter and is involved in phosphate transport but not in regulation of the pho regulon.
J Bacteriol: 1997, 179(8);2534-9
[PubMed:9098050] [WorldCat.org] [DOI] (P p)