Difference between revisions of "Psd"

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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
 
{{SubtiWiki category|[[biosynthesis of lipids]]}},
 
{{SubtiWiki category|[[biosynthesis of lipids]]}},
{{SubtiWiki category|[[cell envelope stress proteins (controlled by SigM, W, X, Y)]]}}
+
{{SubtiWiki category|[[cell envelope stress proteins (controlled by SigM, W, X, Y)]]}},
 +
{{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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=== Additional information===
 
=== Additional information===
 
 
 
  
 
=The protein=
 
=The protein=
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* '''Interactions:'''
 
* '''Interactions:'''
  
* '''Localization:'''
+
* '''Localization:''' cell membrane at the septum {{PubMed|15743965}}
  
 
=== Database entries ===
 
=== Database entries ===
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=References=
 
=References=
  
<pubmed>14762009,18820022,9422599 , </pubmed>
+
<pubmed>14762009,18820022,9422599 , 15743965</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 14:41, 30 March 2011

  • Description: phosphatidylserine decarboxylase

Gene name psd
Synonyms
Essential no
Product phosphatidylserine decarboxylase
Function biosynthesis of phospholipids
Metabolic function and regulation of this protein in SubtiPathways:
Lipid synthesis
MW, pI 29 kDa, 7.27
Gene length, protein length 789 bp, 263 aa
Immediate neighbours ybfM, ybfN
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
Psd context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

biosynthesis of lipids, cell envelope stress proteins (controlled by SigM, W, X, Y), membrane proteins

This gene is a member of the following regulons

SigX regulon

The gene

Basic information

  • Locus tag: BSU02290

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Phosphatidyl-L-serine = phosphatidylethanolamine + CO2 (according to Swiss-Prot)
  • Protein family: Type 1 subfamily (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: [3]

Additional information

Expression and regulation

  • 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

Letal I Salzberg, John D Helmann
Phenotypic and transcriptomic characterization of Bacillus subtilis mutants with grossly altered membrane composition.
J Bacteriol: 2008, 190(23);7797-807
[PubMed:18820022] [WorldCat.org] [DOI] (I 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)

Min Cao, John D Helmann
The Bacillus subtilis extracytoplasmic-function sigmaX factor regulates modification of the cell envelope and resistance to cationic antimicrobial peptides.
J Bacteriol: 2004, 186(4);1136-46
[PubMed:14762009] [WorldCat.org] [DOI] (P p)

K Matsumoto, M Okada, Y Horikoshi, H Matsuzaki, T Kishi, M Itaya, I Shibuya
Cloning, sequencing, and disruption of the Bacillus subtilis psd gene coding for phosphatidylserine decarboxylase.
J Bacteriol: 1998, 180(1);100-6
[PubMed:9422599] [WorldCat.org] [DOI] (P p)