Difference between revisions of "PssA"

From SubtiWiki
Jump to: navigation, search
Line 14: Line 14:
|style="background:#ABCDEF;" align="center"|'''Function''' || biosynthesis of phospholipids  
|style="background:#ABCDEF;" align="center"|'''Function''' || biosynthesis of phospholipids  
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/fatty_acid_syn.html Lipid synthesis]'''
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/fatty_acid_synthesis.html Lipid synthesis]'''
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 19 kDa, 7.881   
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 19 kDa, 7.881   

Revision as of 14:16, 7 March 2010

  • 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
PssA context.gif
This image was kindly provided by SubtiList

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:
  • Interactions:
  • Localization: cell membrane (according to Swiss-Prot)

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



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)

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)