| Description | This entry represents one of the major backbone units of Gram-positive pili, such as those from S.pneumoniae [ ]. There are three major pilin subunits that form the polymeric backbone of the pilin from S. pneumoniae, constructed of three transthyretin-like, CnaB, domains along with a crucial N-terminal domain, D1. The three Cna-B like domains are stabilised by internal Lys-Asn isopeptdie bonds, Gram-positive pili are formed from a single chain of covalently linked subunit proteins (pilins), usually comprising an adhesin at the distal tip, a major pilin that forms the polymer shaft and a minor pilin that mediates cell wall anchoring at the base [].Trypsin-resistant surface T6 protein N-terminal exhibits features of a typical signal sequence and the C-terminal segment is homologue to the membrane anchor region of other gram-positive surface proteins [ ]. The T6 pilin lysine, essential for polymerization, is located in a novel VAKS motif that is structurally homologous to the canonical YPKN pilin lysine in other three- and four-domain Gram-positive pilins. Structurally, T6 has also a conserved pilin core whose surface is decorated with variable loops and extensions []. | Name | Gram-positive pilin backbone subunit 2, Cna-B-like domain |
| Short Name | GramPos_pilinBB | Type | Domain |
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