| http://purl.uniprot.org/citations/22037399 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22037399 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22037399 | http://www.w3.org/2000/01/rdf-schema#comment | "Multiple new prokaryotic C-terminal protein-sorting signals were found that reprise the tripartite architecture shared by LPXTG and PEP-CTERM: motif, TM helix, basic cluster. Defining hidden Markov models were constructed for all. PGF-CTERM occurs in 29 archaeal species, some of which have more than 50 proteins that share the domain. PGF-CTERM proteins include the major cell surface protein in Halobacterium, a glycoprotein with a partially characterized diphytanylglyceryl phosphate linkage near its C terminus. Comparative genomics identifies a distant exosortase homolog, designated archaeosortase A (ArtA), as the likely protein-processing enzyme for PGF-CTERM. Proteomics suggests that the PGF-CTERM region is removed. Additional systems include VPXXXP-CTERM/archeaosortase B in two of the same archaea and PEF-CTERM/archaeosortase C in four others. Bacterial exosortases often fall into subfamilies that partner with very different cohorts of extracellular polymeric substance biosynthesis proteins; several species have multiple systems. Variant systems include the VPDSG-CTERM/exosortase C system unique to certain members of the phylum Verrucomicrobia, VPLPA-CTERM/exosortase D in several alpha- and deltaproteobacterial species, and a dedicated (single-target) VPEID-CTERM/exosortase E system in alphaproteobacteria. Exosortase-related families XrtF in the class Flavobacteria and XrtG in Gram-positive bacteria mark distinctive conserved gene neighborhoods. A picture emerges of an ancient and now well-differentiated superfamily of deeply membrane-embedded protein-processing enzymes. Their target proteins are destined to transit cellular membranes during their biosynthesis, during which most undergo additional posttranslational modifications such as glycosylation."xsd:string |
| http://purl.uniprot.org/citations/22037399 | http://purl.org/dc/terms/identifier | "doi:10.1128/jb.06026-11"xsd:string |
| http://purl.uniprot.org/citations/22037399 | http://purl.org/dc/terms/identifier | "doi:10.1128/jb.06026-11"xsd:string |
| http://purl.uniprot.org/citations/22037399 | http://purl.uniprot.org/core/author | "Haft D.H."xsd:string |
| http://purl.uniprot.org/citations/22037399 | http://purl.uniprot.org/core/author | "Haft D.H."xsd:string |
| http://purl.uniprot.org/citations/22037399 | http://purl.uniprot.org/core/author | "Selengut J.D."xsd:string |
| http://purl.uniprot.org/citations/22037399 | http://purl.uniprot.org/core/author | "Selengut J.D."xsd:string |
| http://purl.uniprot.org/citations/22037399 | http://purl.uniprot.org/core/author | "Payne S.H."xsd:string |
| http://purl.uniprot.org/citations/22037399 | http://purl.uniprot.org/core/author | "Payne S.H."xsd:string |
| http://purl.uniprot.org/citations/22037399 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/22037399 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/22037399 | http://purl.uniprot.org/core/name | "J. Bacteriol."xsd:string |
| http://purl.uniprot.org/citations/22037399 | http://purl.uniprot.org/core/name | "J. Bacteriol."xsd:string |
| http://purl.uniprot.org/citations/22037399 | http://purl.uniprot.org/core/pages | "36-48"xsd:string |
| http://purl.uniprot.org/citations/22037399 | http://purl.uniprot.org/core/pages | "36-48"xsd:string |
| http://purl.uniprot.org/citations/22037399 | http://purl.uniprot.org/core/title | "Archaeosortases and exosortases are widely distributed systems linking membrane transit with posttranslational modification."xsd:string |
| http://purl.uniprot.org/citations/22037399 | http://purl.uniprot.org/core/title | "Archaeosortases and exosortases are widely distributed systems linking membrane transit with posttranslational modification."xsd:string |
| http://purl.uniprot.org/citations/22037399 | http://purl.uniprot.org/core/volume | "194"xsd:string |
| http://purl.uniprot.org/citations/22037399 | http://purl.uniprot.org/core/volume | "194"xsd:string |
| http://purl.uniprot.org/citations/22037399 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/22037399 |
| http://purl.uniprot.org/citations/22037399 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/22037399 |
| http://purl.uniprot.org/citations/22037399 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/22037399 |
| http://purl.uniprot.org/citations/22037399 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/22037399 |