Difference between revisions of "PgsA"

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(References)
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= Categories containing this gene/protein =
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{{SubtiWiki category|[[biosynthesis of lipids]]}},
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{{SubtiWiki category|[[essential genes]]}},
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{{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
PgsA context.gif
This image was kindly provided by SubtiList









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:
  • 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

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)