Exosortase
Transmembrane exosortase (Exosortase_EpsH) | |||||||||
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Identifiers | |||||||||
Symbol | Exosortase_EpsH | ||||||||
Pfam | PF09721 | ||||||||
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Exosortase refers to a family of integral membrane proteins that occur in Gram-negative bacteria and that recognize and cleave the carboxyl-terminal sorting signal PEP-CTERM.[1][2] The name derives from a predicted role analogous to sortase, despite the lack any detectable sequence homology, and a strong association of exosortase genes with exopolysaccharide or extracellular polymeric substance biosynthesis loci. Some archaea have an archaeosortase, related to exosortase rather than to sortases. Archaeosortase A recognizes the signal PGF-CTERM, found at the C-terminus of some archaeal S-layer proteins.
Exosortase has not itself been characterized biochemically. However, recent site-directed mutagenesis work on archaeosortase A, an archaeal homolog of exosortases, strongly supports the notion of a Cys active site and convergent evolution with the sortases. [3]
References
- ^ Haft DH, Paulsen IT, Ward N, Selengut JD (August 2006). "Exopolysaccharide-associated protein sorting in environmental organisms: the PEP-CTERM/EpsH system. Application of a novel phylogenetic profiling heuristic". BMC Biology. 4: 29. doi:10.1186/1741-7007-4-29. PMC 1569441. PMID 16930487.
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: CS1 maint: unflagged free DOI (link) - ^ Haft DH, Payne SH, Selengut JD (January 2012). "Archaeosortases and exosortases are widely distributed systems linking membrane transit with posttranslational modification". Journal of Bacteriology. 194 (1): 36–48. doi:10.1128/JB.06026-11. PMC 3256604. PMID 22037399.
- ^ Abdul Halim MF, Rodriguez R, Stoltzfus JD, Duggin IG, Pohlschroder M (May 2018). "Conserved residues are critical for Haloferax volcanii archaeosortase catalytic activity: Implications for convergent evolution of the catalytic mechanisms of non-homologous sortases from archaea and bacteria". Molecular Microbiology. 108 (3): 276–287. doi:10.1111/mmi.13935. PMID 29465796.