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The translocation and assembly module (TAM) in bacteria consists of TamA and TamB that form a complex to control the transport and secretion of outer membrane proteins. Herein, we demonstrated that the DR_1462-DR_1461-DR_1460 gene loci on chromosome 1 of  Deinococcus radiodurans , which lacks  tamA  homologs, is a  tamB  homolog (DR_146T) with two  tamB  motifs and a DUF490 motif. Mutation of DR_146T resulted in cell envelope peeling and a decrease in resistance to shear stress and osmotic pressure, as well as an increase in oxidative stress resistance, consistent with the phenotype of a surface layer (S-layer) protein SlpA (DR_2577) mutant, demonstrating the involvement of DR_146T in maintenance of cell envelope integrity. The 123 kDa SlpA was absent and only its fragments were present in the cell envelope of DR_146T mutant, suggesting that DR_146T might be involved in maintenance of the S-layer. A mutant lacking the DUF490 motif displayed only a slight alteration in phenotype compared with the wild type, suggesting DUF490 is less important than  tamB  motif for the function of DR_146T. These findings enhance our understanding of the properties of the multilayered envelope in extremophilic  D. radiodurans , as well as the diversity and functions of TAMs in bacteria.

A tamB homolog is involved in maintenance of cell envelope integrity and stress resistance of Deinococcus radiodurans