PssA

• Description: phosphatidylserine synthase
  
  

Gene name	pssA
Synonyms	pss
Essential	no
Product	phosphatidylserine synthase
Function	biosynthesis of phospholipids
Gene expression levels in SubtiExpress: pssA
Metabolic function and regulation of this protein in SubtiPathways: pssA
MW, pI	19 kDa, 7.881
Gene length, protein length	531 bp, 177 aa
Immediate neighbours	ybfK, ybfM
Sequences	Protein DNA DNA_with_flanks
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)