Difference between revisions of "PgsA"
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=== Database entries === | === Database entries === | ||
| + | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU16920&redirect=T BSU16920] | ||
* '''DBTBS entry:''' no entry | * '''DBTBS entry:''' no entry | ||
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=== Database entries === | === Database entries === | ||
| + | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU16920&redirect=T BSU16920] | ||
* '''Structure:''' | * '''Structure:''' | ||
Revision as of 13:46, 2 April 2014
- Description: phosphatidylglycerophosphate synthase
| Gene name | pgsA |
| Synonyms | ymfN |
| Essential | yes PubMed |
| Product | phosphatidylglycerophosphate synthase |
| Function | biosynthesis of phospholipids |
| Gene expression levels in SubtiExpress: pgsA | |
| Metabolic function and regulation of this protein in SubtiPathways: pgsA | |
| MW, pI | 21 kDa, 5.163 |
| Gene length, protein length | 579 bp, 193 aa |
| Immediate neighbours | rodZ, cinA |
| 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
biosynthesis of lipids, essential genes, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU16920
Phenotypes of a mutant
- some point mutations resulting in reduced PgsA activity lead to daptomycin resistance PubMed
essential PubMed
Database entries
- BsubCyc: BSU16920
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
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:
- Localization: cell membrane at the septum PubMed
Database entries
- BsubCyc: BSU16920
- Structure:
- UniProt: P46322
- KEGG entry: [2]
- E.C. number: 2.7.8.5
Additional information
Expression and regulation
- Operon:
- Sigma factor:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Anna-Barbara Hachmann, Elif Sevim, Ahmed Gaballa, David L Popham, Haike Antelmann, John D Helmann
Reduction in membrane phosphatidylglycerol content leads to daptomycin resistance in Bacillus subtilis.
Antimicrob Agents Chemother: 2011, 55(9);4326-37
[PubMed:21709092]
[WorldCat.org]
[DOI]
(I p)
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)
Ayako Nishibori, Jin Kusaka, Hiroshi Hara, Masato Umeda, Kouji Matsumoto
Phosphatidylethanolamine domains and localization of phospholipid synthases in Bacillus subtilis membranes.
J Bacteriol: 2005, 187(6);2163-74
[PubMed:15743965]
[WorldCat.org]
[DOI]
(P p)
