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archaeosortase
An archaeosortase is a protein that occurs in the cell membranes of some archaea. Archaeosortases recognize and remove carboxyl-terminal protein sorting signals about 25 amino acids long from secreted proteins. A genome that encodes one archaeosortase may encode over fifty target proteins. The best characterized archaeosortase target is the Haloferax volcanii S-layer glycoprotein, an extensively modified protein with O-linked glycosylations, N-linked glycosylations, and a large prenyl-derived lipid modification toward the C-terminus. It remains unclear if archaeosortase is a protease that simply removes the C-terminal segment , or a transpeptidase that attaches a lipid moiety in its place.
Archaeosortases are related to exosortases, their counterparts in Gram-negative bacteria. The names of both families of proteins reflect roles analogous to sortases in Gram-positive bacteria, with which they share no sequence homology. The sequences of archaeosortases and exosortases consists mostly of hydrophobic transmembrane helices, which sortases lack. Archaeosortases fall into a number of distinct subtypes, each responsible for recognizing sorting signals with a different signature motif. Archaeosortase A (ArtA) recognizes the PGF-CTERM signal, ArtB recognizes VPXXXP-CTERM, AtrC recognizes PEF-CTERM, and so on; one archaeal genome may encode two different archaeosortase systems.
==References==
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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