[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/archaeosortase-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki24\/archaeosortase-wikipedia\/","headline":"Archaeosortase – Wikipedia","name":"Archaeosortase – Wikipedia","description":"before-content-x4 From Wikipedia, the free encyclopedia after-content-x4 Protein family An archaeosortase is a protein that occurs in the cell membranes","datePublished":"2022-08-20","dateModified":"2022-08-20","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/","image":{"@type":"ImageObject","@id":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","url":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","height":96,"width":96}},"publisher":{"@type":"Organization","name":"Enzyklop\u00e4die","logo":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":600,"height":60}},"image":{"@type":"ImageObject","@id":"https:\/\/en.wikipedia.org\/wiki\/Special:CentralAutoLogin\/start?type=1x1","url":"https:\/\/en.wikipedia.org\/wiki\/Special:CentralAutoLogin\/start?type=1x1","height":"1","width":"1"},"url":"https:\/\/wiki.edu.vn\/en\/wiki24\/archaeosortase-wikipedia\/","wordCount":1862,"articleBody":"     (adsbygoogle = window.adsbygoogle || []).push({});before-content-x4From Wikipedia, the free encyclopedia       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Protein familyAn archaeosortase is a protein that occurs in the cell membranes of some archaea.[1] 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.[2] Knockout of the archaeosortase A (artA) gene, or permutation of the motif Pro-Gly-Phe (PGF) to Pro-Phe-Gly in the S-layer glycoprotein, blocks attachment of the lipid moiety as well as blocking removal of the PGF-CTERM protein-sorting domain.[3]  Thus archaeosortase appears to be a transpeptidase, like sortase, rather than a simple protease.       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Archaeosortases are related to exosortases, their uncharacterized 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.Invariant residues shared by all archaeosortases and exosortases include a Cys and an Arg. Replacement of either destroys catalytic activity, suggesting convergent evolution of the active site with the sortases.[4]In the archaeal model species Haloferax volcanii, archaeosortase A belongs to a fairly large collection of identified membrane-associated proteases, but apparently also to the smaller set of intramembrane cleaving proteases, along with the rhomboid protease RhoII, and in contrast to bacterial sortases.[5]References[edit]^ Haft, Daniel H.; Samuel H. Payne; Jeremy D. Selengut (January 2012). “Archaeosortases and Exosortases Are Widely Distributed Systems Linking Membrane Transit with Posttranslational Modification”. J. Bacteriol. 194 (1): 36\u201348. doi:10.1128\/JB.06026-11. PMC\u00a03256604. PMID\u00a022037399.^ Abdul Halim, Mohd Farid; Pfeiffer, Friedhelm; Zou, James; Frisch, Andrew; Haft, Daniel; Wu, Si; Toli\u0107, Nikola; Brewer, Heather; Payne, Samuel H.; Pa\u0161a-Toli\u0107, Ljiljana; Pohlschroder, Mechthild (Jun 2013). “Haloferax volcanii archaeosortase is required for motility, mating, and C-terminal processing of the S-layer glycoprotein”. Mol Microbiol. 88 (6): 1164\u201375. doi:10.1111\/mmi.12248. PMID\u00a023651326. S2CID\u00a05756916.^ Abdul Halim, MF; Karch, KR; Zhou, Y; Haft, DH; Garcia, BA; Pohlschroder, M (2016). “Permuting the PGF Signature Motif Blocks both Archaeosortase-Dependent C-Terminal Cleavage and Prenyl Lipid Attachment for the Haloferax volcanii S-Layer Glycoprotein”. J. Bacteriol. 198 (5): 808\u201315. doi:10.1128\/JB.00849-15. PMC\u00a04810604. PMID\u00a026712937.^ 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\u2013287. doi:10.1111\/mmi.13935. PMID\u00a029465796.^ Gim\u00e9nez MI, Cerletti M, De Castro RE (2015). “Archaeal membrane-associated proteases: insights on Haloferax volcanii and other haloarchaea”. Frontiers in Microbiology. 6: 39. doi:10.3389\/fmicb.2015.00039. PMC\u00a04343526. PMID\u00a025774151.       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