plsX

168

acyl-acyl carrier protein (ACP):phosphate acyltransferase, catalyzes the synthesis of the intermediate fatty acyl-phosphate (acyl-PO₄)

Locus: BSU_15890

Molecular weight: 35.61 kDa

Isoelectric point: 5.49

Protein length: 333 aa

Gene length: 1002 bp

Function: biosynthesis of phospholipids

Product: acyl-acyl carrier protein (ACP):phosphate acyltransferase

Essential: yes

E.C.: 2.3.1.n2

Synonyms: plsX, ylpD

Genomic Context

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List of homologs in different organisms, belongs to COG0416 (Galperin et al., 2021)

Gene

Coordinates: 1,662,547  1,663,548

Phenotypes of a mutant

• essential PubMed
• depletion results in sporulation deficiency (via SpoIIR) PubMed
• a ts mutant forms an abberant Z-ring and has a cell division defect PubMed
• depletion results in accumulation of malonyl-CoA and of long-chain-ACPs PubMed

The protein

Catalyzed reaction/ biological activity

• catalyzes the synthesis of the intermediate fatty acyl-phosphate (acyl-PO₄)
• fatty acyl-[ACP] + phosphate --> acyl phosphate + holo-[ACP] (according to UniProt)

Protein family

• plsX family (single member, according to UniProt)

Structure

• 1VI1 (PDB) PubMed
• 6A1K (PDB) PubMed
• P71018 (AlphaFold)

Localization

• localizes to regions of increased fluidity in the membrane (via a short amphipathic α-peptide) PubMed
• uniformly distributed on the membrane of most cells, but occasionally appears as membrane foci as well PubMed
• in the presence of daptomycin, PlsX delocalizes from the membrane to the cytoplasm PubMed

Expression and Regulation

Operons

• Genes: fapR-plsX-fabD-fabG-acpA

  Description: PubMed

  Regulation

  • ''FapR'': repressed in the absence of malonyl-CoA or malonyl-ACP (FapR) PubMed
  • expression is reduced in motile cells as compared to non-motile cells PubMed

  Regulatory mechanism

  • FapR: repression, PubMed, in fapR regulon
  • ComA: activation, (ComA) PubMed, in comA regulon

  Sigma factors

  • SigA: sigma factor, PubMed, in sigA regulon

Biological materials

Two-hybrid system

• B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Matsumoto lab PubMed

References

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