Difference between revisions of "PgsA"
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+ | = Categories containing this gene/protein = | ||
+ | {{SubtiWiki category|[[biosynthesis of lipids]]}}, | ||
+ | {{SubtiWiki category|[[essential genes]]}}, | ||
+ | {{SubtiWiki category|[[membrane proteins]]}} | ||
=The protein= | =The protein= | ||
Revision as of 18:46, 30 November 2010
- Description: phosphatidylglycerophosphate synthase
Gene name | pgsA |
Synonyms | ymfN |
Essential | yes PubMed |
Product | phosphatidylglycerophosphate synthase |
Function | biosynthesis of phospholipids |
Metabolic function and regulation of this protein in SubtiPathways: Lipid synthesis | |
MW, pI | 21 kDa, 5.163 |
Gene length, protein length | 579 bp, 193 aa |
Immediate neighbours | rodZ, cinA |
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: BSU16920
Phenotypes of a mutant
essential PubMed
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
Categories containing this gene/protein
biosynthesis of lipids, essential genes, membrane proteins
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: CDP-diacylglycerol + sn-glycerol 3-phosphate = CMP + 3(3-sn-phosphatidyl)-sn-glycerol 1-phosphate (according to Swiss-Prot)
- Protein family: CDP-alcohol phosphatidyltransferase class-I family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: cell membrane PubMed
Database entries
- Structure:
- UniProt: P46322
- KEGG entry: [2]
- E.C. number: 2.7.8.5
Additional information
Expression and regulation
- Operon:
- 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
Jessica C Zweers, Thomas Wiegert, Jan Maarten van Dijl
Stress-responsive systems set specific limits to the overproduction of membrane proteins in Bacillus subtilis.
Appl Environ Microbiol: 2009, 75(23);7356-64
[PubMed:19820159]
[WorldCat.org]
[DOI]
(I p)
Michihiro Hashimoto, Hiroaki Takahashi, Yoshinori Hara, Hiroshi Hara, Kei Asai, Yoshito Sadaie, Kouji Matsumoto
Induction of extracytoplasmic function sigma factors in Bacillus subtilis cells with membranes of reduced phosphatidylglycerol content.
Genes Genet Syst: 2009, 84(3);191-8
[PubMed:19745567]
[WorldCat.org]
[DOI]
(P p)
Claudia S López, Alejandro F Alice, Horacio Heras, Emilio A Rivas, Carmen Sánchez-Rivas
Role of anionic phospholipids in the adaptation of Bacillus subtilis to high salinity.
Microbiology (Reading): 2006, 152(Pt 3);605-616
[PubMed:16514141]
[WorldCat.org]
[DOI]
(P p)