Difference between revisions of "PssA"
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* '''Operon:''' ''[[pssA]]-[[ybfM]]-[[psd]]'' {{PubMed|14762009}} | * '''Operon:''' ''[[pssA]]-[[ybfM]]-[[psd]]'' {{PubMed|14762009}} | ||
| − | * '''[ | + | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=pssA_247744_248277_1 pssA] {{PubMed|22383849}} |
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| + | * '''Sigma factor:''' [[SigA]] {{PubMed|14762009}}, [[SigX]] {{PubMed|14762009}} | ||
* '''Regulation:''' | * '''Regulation:''' | ||
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* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
| − | * '''Additional information:''' | + | * '''Additional information:''' |
=Biological materials = | =Biological materials = | ||
Revision as of 15:06, 7 August 2012
- Description: phosphatidylserine synthase
| Gene name | pssA |
| Synonyms | pss |
| Essential | no |
| Product | phosphatidylserine synthase |
| Function | biosynthesis of phospholipids |
| Metabolic function and regulation of this protein in SubtiPathways: Lipid synthesis | |
| MW, pI | 19 kDa, 7.881 |
| Gene length, protein length | 531 bp, 177 aa |
| Immediate neighbours | ybfK, ybfM |
| 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, V, W, X, Y), membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU02270
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: CDP-diacylglycerol + L-serine = CMP + (3-sn-phosphatidyl)-L-serine (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
- Structure:
- UniProt: P39823
- KEGG entry: [3]
- E.C. number: 2.7.8.8
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
Reviews
Original publications
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)
S K Saha, Y Furukawa, H Matsuzaki, I Shibuya, K Matsumoto
Directed mutagenesis, Ser-56 to Pro, of Bacillus subtilis phosphatidylserine synthase drastically lowers enzymatic activity and relieves amplification toxicity in Escherichia coli.
Biosci Biotechnol Biochem: 1996, 60(4);630-3
[PubMed:8829529]
[WorldCat.org]
[DOI]
(P p)
