Edge Rewrite
// HTMLRewriter · presentation

This page was redesigned at the edge.

Cloudflare fetched the original article and streamed it through HTMLRewriter to apply an entirely new visual system without rebuilding the source page.

// request.cf · coarse context

A page that knows where it met you.

Only coarse request metadata is shown. This demo does not display or persist visitor IP addresses.

Country
US
Cloudflare location
CMH
Connection
HTTP/2
Language
Not provided

Ray ID: a23cfa3e7fae34fc

Jump to content

Exosortase

From Wikipedia, the free encyclopedia
Transmembrane exosortase (Exosortase_EpsH)
Identifiers
SymbolExosortase_EpsH
PfamPF09721
Available protein structures:
PDB  PF09721 (ECOD; PDBsum)  
AlphaFold

Exosortase refers to a family of integral membrane proteins that occur in Gram-negative bacteria that recognizes and cleaves the carboxyl-terminal sorting signal PEP-CTERM.[1][2] The name derives from a predicted role analogous to sortase, despite the lack of any detectable sequence homology, and a strong association of exosortase genes with exopolysaccharide or extracellular polymeric substance biosynthesis loci. Many archaea have an archaeosortase, homologous to exosortases rather than to sortases. Archaeosortase A recognizes the signal PGF-CTERM, found at the C-terminus of some archaeal S-layer proteins. Following processing by archaeosortase A, the PGF-CTERM region is gone, and a prenyl-derived lipid anchor is present at the C-terminus instead.

Exosortase has not itself been characterized biochemically. However, 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 sortase family transpeptidases.[3] In 2018, a study on Zoogloea resiniphila, a bacterium found in activated sludge wastewater treatment plants, showed that PEP-CTERM proteins (and by implication, exosortase as well) are essential to floc formation in some systems.[4] More recently, Parrett, et al. {{PMID:40358234}} showed that cyanoexosortase B, the lone exosortase in the filamentous Cyanobacterium Nostoc punctiforme, is required both for a colony gliding behavior and for completion of the biosynthesis of the UV-absorbing pigment scytonemin. Both processes depend on PEP-CTERM proteins.

References

[edit]
  1. 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.
  2. 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.
  3. 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.
  4. Gao N, Xia M, Dai J, Yu D, An W, Li S, Liu S, He P, Zhang L, Wu Z, Bi X, Chen S, Haft DH, Qiu D (May 2018). "Both widespread PEP-CTERM proteins and exopolysaccharides are required for floc formation of Zoogloea resiniphila and other activated sludge bacteria". Environmental Microbiology. 20 (5): 1677–1692. Bibcode:2018EnvMi..20.1677G. doi:10.1111/1462-2920.14080. PMID 29473278. S2CID 4341022. Archived from the original on 2021-01-21. Retrieved 2019-12-14.