PhoR

• 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

Database entries

• BsubCyc: BSU29100

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Interactions: PhoP-PhoR

• Localization:

Database entries

• BsubCyc: BSU29100

• Structure: 3CWF (extracellular PAS domain) PubMed

• UniProt: P23545

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: phoP-phoR PubMed

• Expression browser: 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:
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 453 PubMed

Biological materials

• Mutant:
  • 1A966 ( phoR::tet), PubMed, available at BGSC

• 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

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)