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8.A.35 The Mycobacterial Membrane Protein Small (MmpS) Family

The MmpS family (mycobacterial membrane protein small) includes over 100 small membrane proteins specific to the genus Mycobacterium that have not yet been studied experimentally. The genes encoding MmpS proteins are often associated with mmpL genes, which are homologous to the RND (resistance nodulation cell division) genes of Gram-negative bacteria that encode proteins functioning as multidrug efflux system. Deshayes et al. (2010) showed by molecular genetics and biochemical analysis that MmpS4 in Mycobacterium smegmatis is required for the production and export of large amounts of cell surface glycolipids, but is dispensable for biosynthesis per se. MmpS4 is dispensable for transport to the surface. Orthologous complementation demonstrated that the MmpS4 proteins are exchangeable, thus not specific to a defined lipid species. MmpS4 function requires the formation of a protein complex at the pole of the bacillus, which requires the extracytosolic C-terminal domain of MmpS4. Deshayes et al. (2010) suggested that MmpS proteins facilitate lipid biosynthesis by acting as a scaffold for coupled biosynthesis and transport machinery.

References associated with 8.A.35 family:

Briffotaux, J., W. Huang, X. Wang, and B. Gicquel. (2017). MmpS5/MmpL5 as an efflux pump in Mycobacterium species. Tuberculosis (Edinb) 107: 13-19. 29050760
Deshayes, C., H. Bach, D. Euphrasie, R. Attarian, M. Coureuil, W. Sougakoff, F. Laval, Y. Av-Gay, M. Daffé, G. Etienne, and J.M. Reyrat. (2010). MmpS4 promotes glycopeptidolipids biosynthesis and export in Mycobacterium smegmatis. Mol. Microbiol. 78: 989-1003. 21062372
Gupta, K.R., C.M. Gwin, K.C. Rahlwes, K.J. Biegas, C. Wang, J.H. Park, J. Liu, B.M. Swarts, Y.S. Morita, and E.H. Rego. (2022). An essential periplasmic protein coordinates lipid trafficking and is required for asymmetric polar growth in mycobacteria. Elife 11:. [Epub: Ahead of Print] 36346214
Rego, E.H., R.E. Audette, and E.J. Rubin. (2017). Deletion of a mycobacterial divisome factor collapses single-cell phenotypic heterogeneity. Nature 546: 153-157. 28569798
Wells, R.M., C.M. Jones, Z. Xi, A. Speer, O. Danilchanka, K.S. Doornbos, P. Sun, F. Wu, C. Tian, and M. Niederweis. (2013). Discovery of a siderophore export system essential for virulence of Mycobacterium tuberculosis. PLoS Pathog 9: e1003120. 23431276