PssA

• 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
Expression at a glance   PubMed

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

SigX regulon

The gene

Basic information

• Locus tag: BSU02270

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Interactions:

• Localization:
  • cell membrane at the septum PubMed

Database entries

• Structure:

• UniProt: P39823

• KEGG entry: [3]

• E.C. number: 2.7.8.8

Expression and regulation

• Operon: pssA-ybfM-psd PubMed

• Expression browser: pssA PubMed

• Sigma factor: SigA PubMed, SigX PubMed

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

K Matsumoto
Phosphatidylserine synthase from bacteria.
Biochim Biophys Acta: 1997, 1348(1-2);214-27
[PubMed:9370336] [WorldCat.org] [DOI] (P p)

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)