Difference between revisions of "GdpP"
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= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
| − | {{SubtiWiki category|[[metabolism of signalling nucleotides]]}} | + | {{SubtiWiki category|[[metabolism of signalling nucleotides]]}}, |
| + | {{SubtiWiki category|[[membrane proteins]]}} | ||
| + | |||
= This gene is a member of the following [[regulons]] = | = This gene is a member of the following [[regulons]] = | ||
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===Phenotypes of a mutant === | ===Phenotypes of a mutant === | ||
* inactivation of ''[[gdpP]]'' strongly restores beta-lactam resistance in a ''[[sigM]]'' mutant {{PubMed|22211522}} | * inactivation of ''[[gdpP]]'' strongly restores beta-lactam resistance in a ''[[sigM]]'' mutant {{PubMed|22211522}} | ||
| + | |||
=== Database entries === | === Database entries === | ||
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU40510&redirect=T BSU40510] | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU40510&redirect=T BSU40510] | ||
| Line 78: | Line 81: | ||
* '''Kinetic information:''' | * '''Kinetic information:''' | ||
| − | * '''Domains:''' | + | * '''[[Domains]]:''' |
| − | ** N- | + | ** two transmembrane domains at the N-terminus |
| + | ** a domain that shares minimum sequence homology with Heme-binding [[PAS domain|Per-ARNT-Sim (PAS) domains]] (80 aa) {{PubMed|21257773}} | ||
** degenerate GGDEF domain (aa 173 - 301) {{PubMed|22211522}} | ** degenerate GGDEF domain (aa 173 - 301) {{PubMed|22211522}} | ||
** DHH/ DHHA1 phosphodiesterase domain {{PubMed|22211522}} | ** DHH/ DHHA1 phosphodiesterase domain {{PubMed|22211522}} | ||
Revision as of 14:34, 25 February 2015
- Description: cyclic di-AMP phosphodiesterase
| Gene name | gdpP |
| Synonyms | yybT |
| Essential | no |
| Product | c-di-AMP phosphodiesterase |
| Function | control of sporulation initiation, cell wall homeostasis |
| Gene expression levels in SubtiExpress: gdpP | |
| Metabolic function and regulation of this protein in SubtiPathways: GdpP | |
| MW, pI | 74 kDa, 4.865 |
| Gene length, protein length | 1977 bp, 659 aa |
| Immediate neighbours | rplI, yybS |
| Sequences | Protein DNA DNA_with_flanks |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
metabolism of signalling nucleotides, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU40510
Phenotypes of a mutant
Database entries
- BsubCyc: BSU40510
- 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:
- two transmembrane domains at the N-terminus
- a domain that shares minimum sequence homology with Heme-binding Per-ARNT-Sim (PAS) domains (80 aa) PubMed
- degenerate GGDEF domain (aa 173 - 301) PubMed
- DHH/ DHHA1 phosphodiesterase domain PubMed
- Modification:
- Cofactor(s): b-type heme with 1:1 stoichiometry PubMed
- Effectors of protein activity:
Database entries
- BsubCyc: BSU40510
- UniProt: P37484
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Sigma factor:
- Regulation:
- Regulatory mechanism:
Biological materials
- Mutant:
- GP998 (gdpP::spc), available in Jörg Stülke's lab
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Carolina Gándara, Juan C Alonso
DisA and c-di-AMP act at the intersection between DNA-damage response and stress homeostasis in exponentially growing Bacillus subtilis cells.
DNA Repair (Amst): 2015, 27;1-8
[PubMed:25616256]
[WorldCat.org]
[DOI]
(I p)
Edward Tan, Feng Rao, Swathi Pasunooti, Thi Huong Pham, Ishin Soehano, Mark S Turner, Chong Wai Liew, Julien Lescar, Konstantin Pervushin, Zhao-Xun Liang
Solution structure of the PAS domain of a thermophilic YybT protein homolog reveals a potential ligand-binding site.
J Biol Chem: 2013, 288(17);11949-59
[PubMed:23504327]
[WorldCat.org]
[DOI]
(I p)
Yun Luo, John D Helmann
A σD-dependent antisense transcript modulates expression of the cyclic-di-AMP hydrolase GdpP in Bacillus subtilis.
Microbiology (Reading): 2012, 158(Pt 11);2732-2741
[PubMed:22956758]
[WorldCat.org]
[DOI]
(I p)
Yun Luo, John D Helmann
Analysis of the role of Bacillus subtilis σ(M) in β-lactam resistance reveals an essential role for c-di-AMP in peptidoglycan homeostasis.
Mol Microbiol: 2012, 83(3);623-39
[PubMed:22211522]
[WorldCat.org]
[DOI]
(I p)
Yaara Oppenheimer-Shaanan, Ezequiel Wexselblatt, Jehoshua Katzhendler, Eylon Yavin, Sigal Ben-Yehuda
c-di-AMP reports DNA integrity during sporulation in Bacillus subtilis.
EMBO Rep: 2011, 12(6);594-601
[PubMed:21566650]
[WorldCat.org]
[DOI]
(I p)
Feng Rao, Qiang Ji, Ishin Soehano, Zhao-Xun Liang
Unusual heme-binding PAS domain from YybT family proteins.
J Bacteriol: 2011, 193(7);1543-51
[PubMed:21257773]
[WorldCat.org]
[DOI]
(I p)
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)
GdpP homologs in other organisms
Linda M Holland, Sinéad T O'Donnell, Dmitri A Ryjenkov, Larissa Gomelsky, Shawn R Slater, Paul D Fey, Mark Gomelsky, James P O'Gara
A staphylococcal GGDEF domain protein regulates biofilm formation independently of cyclic dimeric GMP.
J Bacteriol: 2008, 190(15);5178-89
[PubMed:18502872]
[WorldCat.org]
[DOI]
(I p)
