Difference between revisions of "PhoR"

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(References)
(Expression and regulation)
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** carbon catabolite repression ([[CcpA]]) {{PubMed|16452408}}
 
** carbon catabolite repression ([[CcpA]]) {{PubMed|16452408}}
 
** expressed under conditions of phosphate limitation ([[PhoP]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/15205429,14762014 PubMed]
 
** expressed under conditions of phosphate limitation ([[PhoP]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/15205429,14762014 PubMed]
 +
** expressed in post-exponential phase ([[ScoC]])  {{PubMed|20382764}}
  
 
* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
** [[CcpA]]: transcription repression {{PubMed|16452408}}
+
** [[CcpA]]: transcription repression {{PubMed|16452408,12850135}}
 
** [[PhoP]]: transcription activation [http://www.ncbi.nlm.nih.gov/sites/entrez/15205429,14762014 PubMed]
 
** [[PhoP]]: transcription activation [http://www.ncbi.nlm.nih.gov/sites/entrez/15205429,14762014 PubMed]
 +
** [[ScoC]]: transcription repression {{PubMed|20382764}}
  
 
* '''Additional information:'''
 
* '''Additional information:'''

Revision as of 11:34, 13 April 2010

  • 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
MW, pI 64 kDa, 5.957
Gene length, protein length 1737 bp, 579 aa
Immediate neighbours polA, phoP
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
PhoR context.gif
This image was kindly provided by SubtiList



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:
  • Localization:

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:

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

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)