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Genomic analyses of  Viridibacillus arvi  JG-B58 that was previously isolated from heavy metal contaminated environment identified three different putative surface layer (S-layer) protein genes namely  slp 1,  slp 2, and  slp 3. All three genes are expressed during cultivation. At least two of the  V .  arvi  JG-B58 S-layer proteins were visualized on the surface of living cells via atomic force microscopy (AFM). These S-layer proteins form a double layer with  p4  symmetry. The S-layer proteins were isolated from the cells using two different methods. Purified S-layer proteins were recrystallized on SiO 2  substrates in order to study the structure of the arrays and self-assembling properties. The primary structure of all examined S-layer proteins lack some features that are typical for  Bacillus  or  Lysinibacillus  S-layers. For example, they possess no SLH domains that are usually responsible for the anchoring of the proteins to the cell wall. Further, the pI values are relatively high ranging from 7.84 to 9.25 for the matured proteins. Such features are typical for S-layer proteins of  Lactobacillus  species although sequence comparisons indicate a close relationship to S-layer proteins of  Lysinibacillus  and  Bacillus  strains. In comparison to the numerous descriptions of S-layers, there are only a few studies reporting the concomitant existence of two different S-layer proteins on cell surfaces. Together with the genomic data, this is the first description of a novel type of S-layer proteins showing features of  Lactobacillus  as well as of  Bacillus -type S-layer proteins and the first study of the cell envelope of  Viridibacillus arvi .

Characterization of Three Different Unusual S-Layer Proteins from Viridibacillus arvi JG-B58 That Exhibits Two Super-Imposed S-Layer Proteins