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) |
| Gene expression levels in SubtiExpress: phoP | |
| 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
| |
Expression at a glance PubMed
| |
Contents
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 PhoP regulon
The gene
Basic information
- Locus tag: BSU29110
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
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
- Localization: cell membrane (according to Swiss-Prot)
Database entries
- Structure: 1MVO (receiver domain)
- UniProt: P13792
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- 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
Regulation of phoP-phoR expression
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)
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)
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)
Biochemical analyses
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)
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)
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)
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)
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)
Targets of PhoR
Additional publications: PubMed
Other original publications
