Difference between revisions of "GdpP"
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− | * '''Operon:''' | + | * '''Operon:''' ''[[yybS]]-[[yybT]]-[[rplI]]'' (according to [http://dbtbs.hgc.jp/COG/prom/yybST-rplI.html DBTBS]) |
* '''[[Sigma factor]]:''' | * '''[[Sigma factor]]:''' | ||
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* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
− | * '''Additional information:''' | + | * '''Additional information:''' |
=Biological materials = | =Biological materials = |
Revision as of 20:47, 11 February 2010
- Description: cyclic dinucleotide phosphodiesterase, involved in stress signaling and response
Gene name | yybT |
Synonyms | |
Essential | no |
Product | cyclic dinucleotide phosphodiesterase |
Function | unknown |
MW, pI | 74 kDa, 4.865 |
Gene length, protein length | 1977 bp, 659 aa |
Immediate neighbours | rplI, yybS |
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: BSU40510
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: cyclic dinucleotide phosphodiesterase, hydrolysis of di-cyclic AMP PubMed
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity: ppGpp inhibits cyclic dinucleotide phosphodiesterase activity PubMed
- Interactions:
- Localization:
Database entries
- Structure:
- UniProt: P37484
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- 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
Feng Rao, Rui Yin See, Dongwei Zhang, Delon Chengxu Toh, Qiang Ji, Zhao-Xun Liang
YybT is a signaling protein that contains a cyclic dinucleotide phosphodiesterase domain and a GGDEF domain with ATPase activity.
J Biol Chem: 2010, 285(1);473-82
[PubMed:19901023]
[WorldCat.org]
[DOI]
(I p)