Difference between revisions of "RapB"
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=Expression and regulation= | =Expression and regulation= | ||
− | * '''Operon:''' | + | * '''Operon:''' ''rapB'' {{PubMed|9353933}} |
− | * '''[[Sigma factor]]:''' | + | * '''[[Sigma factor]]:''' [[SigA]] {{PubMed|11535782}} |
* '''Regulation:''' | * '''Regulation:''' | ||
Line 118: | Line 118: | ||
=References= | =References= | ||
− | <pubmed>8643670,8730857,12067336,9843420,, </pubmed> | + | <pubmed>8643670,8730857,12067336,9843420,11535782 , </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 19:26, 2 February 2010
- Description: response regulator aspartate phosphatase, dephosphorylates Spo0F-P, control of the phosphorelay
Gene name | rapB |
Synonyms | spo0P, ywmE |
Essential | no |
Product | response regulator aspartate phosphatase |
Function | control of sporulation initiation |
MW, pI | 44 kDa, 4.873 |
Gene length, protein length | 1131 bp, 377 aa |
Immediate neighbours | ywmF, moaA |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU36690
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: RAP family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
Database entries
- Structure:
- UniProt: P70962
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: rapB PubMed
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Sophie J Stephenson, Marta Perego
Interaction surface of the Spo0A response regulator with the Spo0E phosphatase.
Mol Microbiol: 2002, 44(6);1455-67
[PubMed:12067336]
[WorldCat.org]
[DOI]
(P p)
Hanne Jarmer, Thomas S Larsen, Anders Krogh, Hans Henrik Saxild, Søren Brunak, Steen Knudsen
Sigma A recognition sites in the Bacillus subtilis genome.
Microbiology (Reading): 2001, 147(Pt 9);2417-2424
[PubMed:11535782]
[WorldCat.org]
[DOI]
(P p)
Y L Tzeng, V A Feher, J Cavanagh, M Perego, J A Hoch
Characterization of interactions between a two-component response regulator, Spo0F, and its phosphatase, RapB.
Biochemistry: 1998, 37(47);16538-45
[PubMed:9843420]
[WorldCat.org]
[DOI]
(P p)
M Perego, P Glaser, J A Hoch
Aspartyl-phosphate phosphatases deactivate the response regulator components of the sporulation signal transduction system in Bacillus subtilis.
Mol Microbiol: 1996, 19(6);1151-7
[PubMed:8730857]
[WorldCat.org]
[DOI]
(P p)
M Perego, J A Hoch
Cell-cell communication regulates the effects of protein aspartate phosphatases on the phosphorelay controlling development in Bacillus subtilis.
Proc Natl Acad Sci U S A: 1996, 93(4);1549-53
[PubMed:8643670]
[WorldCat.org]
[DOI]
(P p)