NMR resonance assignment of the autoimmunity protein SpaI from Bacillus subtilis ATCC 6633

Biomol NMR Assign. 2012 Apr;6(1):9-13. doi: 10.1007/s12104-011-9314-5. Epub 2011 Jun 5.

Abstract

Bacillus subtilis ATCC 6633 produces the lipid II targeting lantibiotic subtilin. For self-protection these gram-positive bacteria express a cluster of four self-immunity proteins named SpaIFEG. SpaI is a 16.8 kDa lipoprotein which is attached to the outside of the cytoplasmic membrane via a covalently linked diacylglycerol anchor. Together with the ABC-transporter SpaFEG, SpaI protects the membrane from subtilin insertion and there is evidence for a direct interaction of SpaI with subtilin. As a prerequisite for further structural studies of SpaI and the SpaI/subtilin complex we report here the full (1)H, (15)N, (13)C chemical shift assignment for a stable 14.9 kDa C-terminal fragment of SpaI.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Autoimmunity*
  • Bacillus subtilis*
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / immunology
  • Lipoproteins / chemistry*
  • Lipoproteins / immunology
  • Membrane Proteins / chemistry*
  • Membrane Proteins / immunology
  • Nuclear Magnetic Resonance, Biomolecular*

Substances

  • Bacterial Proteins
  • Lipoproteins
  • Membrane Proteins
  • SpaI protein, Bacillus subtilis