pfam18641: LidA_Long_CC (This model is not part of the current CDD release)
LidA long coiled-coil domain
LidA, another Rab1-interacting bacterial effector protein, is translocated by Legionella into the host cytosol at the beginning of infection, and it localized to the Legionella-containing vacuole (LCV) at the cytosolic surface. It has been shown that tight interaction with Rab1 allows LidA to facilitate the Legionella targeting factor (DrrA/SidM)-catalyzed release of Rab1 from GDP dissociation inhibitors (GDI). The base of the protein is formed by two antiparallel coiled-coil structures forming a long coiled-coil domain. This region of LidA interacts with switch and interswitch regions of Rab1 the nucleotide binding pocket of Rab8a, hence blocking access to the GDP/GTP-binding site to a great extent.