LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | Repeat |
| Description | Antigen I/II (Ag I/II) family proteins are sortase anchored cell surface adhesins that are nearly ubiquitous across streptococci and contribute to many streptococcal diseases, including dental caries, respiratory tract infections, and meningitis. They appear to be multifunctional adhesins with affinities to various host substrates, acting to mediate attachment to host surfaces and stimulate immune responses from the colonized host. Each of the polypeptides possesses seven structural regions, comprising a signal sequence, a highly charged N-terminal region, an alanine-rich repetitive domain (A region), a globular domain termed the V-domain based on the variability observed in this region between strains, a proline-rich repetitive region (P region), a C-terminal domain, and cell wall-anchoring sequences. proteins adopt a cell wall-anchored stalk structure formed by interactions between the intertwined A- and P-domains, which projects the V-domain containing a binding cleft away from the cell surface. This cleft may be used to promote streptococcal colonization of various tissues via both direct cellular adherence or interaction with extracellular matrix components [ , , ].This entry represents the A region of alanine-rich repeats found in different species of Streptococcus, which forms a long α-helix that intimately intertwines into a left-handed supercoiled structure with the P repeat polyproline II (PPII) helix to form an unusually long and narrow stalk [ , ]. |
| Short Name | Surface_Ag_I_II_A_rpt |
