Difference between revisions of "PhoR"

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* '''Additional information:'''
 
* '''Additional information:'''
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** number of protein molecules per cell (complex medium with amino acids, without glucose): 453 {{PubMed|24696501}}
  
 
=Biological materials =
 
=Biological materials =

Revision as of 10:09, 17 April 2014

  • Description: two-component sensor kinase, regulation of phosphate metabolism

Gene name phoR
Synonyms
Essential no
Product two-component sensor kinase
Function regulation of phosphate metabolism
Gene expression levels in SubtiExpress: phoR
Interactions involving this protein in SubtInteract: PhoR
MW, pI 64 kDa, 5.957
Gene length, protein length 1737 bp, 579 aa
Immediate neighbours polA, phoP
Sequences Protein DNA DNA_with_flanks
Genetic context
PhoR context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PhoR expression.png
























Categories containing this gene/protein

phosphate metabolism, protein modification, transcription factors and their control, 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: BSU29100

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: autophosphorylation, phosphorylation of PhoP
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains: two transmembrane segments, C-terminal histidine phosphotransferase domain
  • Modification: autophosphorylation on a His residue
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 3CWF (extracellular PAS domain) PubMed
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • carbon catabolite repression (CcpA) PubMed
    • expressed under conditions of phosphate limitation (PhoP) PubMed
    • expressed in post-exponential phase (ScoC) PubMed
  • Additional information:
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 453 PubMed

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

Your additional remarks

References

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)

Changsoo Chang, Christine Tesar, Minyi Gu, Gyorgy Babnigg, Andrzej Joachimiak, P Raj Pokkuluri, Hendrik Szurmant, Marianne Schiffer
Extracytoplasmic PAS-like domains are common in signal transduction proteins.
J Bacteriol: 2010, 192(4);1156-9
[PubMed:20008068] [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)

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)

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)

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)

L Shi, F M Hulett
The cytoplasmic kinase domain of PhoR is sufficient for the low phosphate-inducible expression of pho regulon genes in Bacillus subtilis.
Mol Microbiol: 1999, 31(1);211-22
[PubMed:9987123] [WorldCat.org] [DOI] (P p)

Jörg P Müler, Zhidong An, Tarek Merad, Ian C Hancock, Colin R Harwood
Influence of Bacillus subtilis phoR on cell wall anionic polymers.
Microbiology (Reading): 1997, 143 ( Pt 3);947-956
[PubMed:9084179] [WorldCat.org] [DOI] (P p)