| Primary Identifier | IPR041463 | Type | Domain |
| Short Name | LidA_long_CC |
| description | 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 []. |
