Difference between revisions of "PgsA"

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===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
 +
* some point mutations resulting in reduced PgsA activity lead to daptomycin resistance {{PubMed|21709092}}
  
 
essential [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed]
 
essential [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed]
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=References=
 
=References=
<pubmed>19745567 16514141  19820159 15743965 </pubmed>
+
<pubmed>19745567 16514141  19820159 15743965 21709092 </pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 11:17, 29 June 2011

  • 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
PgsA context.gif
This image was kindly provided by SubtiList









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

  • 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:
  • Interactions:
  • Localization: cell membrane at the septum PubMed

Database entries

  • Structure:
  • KEGG entry: [2]

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

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)