Structural highlights
Function
SBMA_ECOLI Uptake of antimicrobial peptides. Required for the transport of microcin B17 (MccB17), microcin 25 (Mcc25) and proline-rich antimicrobial peptides (such as Cathelicidin-3 and Arasin 1) into the cell.[1] [2] [3] [4]
References
- ↑ Mattiuzzo M, Bandiera A, Gennaro R, Benincasa M, Pacor S, Antcheva N, Scocchi M. Role of the Escherichia coli SbmA in the antimicrobial activity of proline-rich peptides. Mol Microbiol. 2007 Oct;66(1):151-63. doi: 10.1111/j.1365-2958.2007.05903.x. Epub, 2007 Aug 28. PMID:17725560 doi:http://dx.doi.org/10.1111/j.1365-2958.2007.05903.x
- ↑ Lavina M, Pugsley AP, Moreno F. Identification, mapping, cloning and characterization of a gene (sbmA) required for microcin B17 action on Escherichia coli K12. J Gen Microbiol. 1986 Jun;132(6):1685-93. PMID:3543211
- ↑ Salomon RA, Farias RN. The peptide antibiotic microcin 25 is imported through the TonB pathway and the SbmA protein. J Bacteriol. 1995 Jun;177(11):3323-5. doi: 10.1128/jb.177.11.3323-3325.1995. PMID:7768835 doi:http://dx.doi.org/10.1128/jb.177.11.3323-3325.1995
- ↑ Paulsen VS, Mardirossian M, Blencke HM, Benincasa M, Runti G, Nepa M, Haug T, Stensvag K, Scocchi M. Inner membrane proteins YgdD and SbmA are required for the complete susceptibility of Escherichia coli to the proline-rich antimicrobial peptide arasin 1(1-25). Microbiology (Reading). 2016 Apr;162(4):601-609. doi: 10.1099/mic.0.000249. PMID:26860543 doi:http://dx.doi.org/10.1099/mic.0.000249
