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Updated: Jun 1, 2026

Identification of Antibacterial Immunity Proteins in Escherichia coli using MALDI-TOF-TOF-MS/MS and Top-Down Proteomic Analysis
Published on: May 23, 2021
NMR resonance assignment of the autoimmunity protein SpaI from Bacillus subtilis ATCC 6633
Nina Alexandra Christ1, Elke Duchardt-Ferner, Stefanie Düsterhus
1Institut für Molekulare Biowissenschaften, Johann-Wolfgang-Goethe-Universität Frankfurt/M., Max-von-Laue-Str. 9, 60438 Frankfurt, Germany.
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.

