Difference between revisions of "Psd"
| Line 35: | Line 35: | ||
= [[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]] =  | ||
| Line 55: | Line 56: | ||
=== Additional information===  | === Additional information===  | ||
| − | |||
| − | |||
| − | |||
=The protein=  | =The protein=  | ||
| Line 83: | Line 81: | ||
* '''Interactions:'''  | * '''Interactions:'''  | ||
| − | * '''Localization:'''  | + | * '''Localization:''' cell membrane at the septum {{PubMed|15743965}}  | 
=== Database entries ===  | === Database entries ===  | ||
| Line 129: | Line 127: | ||
=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  
  This image was kindly provided by SubtiList 
 | |
Contents
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
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:
 
- UniProt: P39822
 
- KEGG entry: [3]
 
- E.C. number: 4.1.1.65
 
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)
