Protein Domain : Internalin I, Ig-like domain IPR044056

Type	Domain
Description	Internalins (Inl) are virulence factors exposed in the surface of many Gram-positive bacteria and are involved in several processes such as recognition of cellular receptors and pathogen entry to escape from autophagy. These surface proteins were found as markers for Listeria monocytogenes species and essential for infection. Internalins are modular proteins composed by the characteristic N-terminal LRR repeats followed by domains that may vary among the members internalins family, explaining the distinct roles they play during infection. LRR repeats are followed by a conserved immunoglobulin-like domain [ ], a variable region that corresponds to MucBP (mucin binding protein) domains, and a C-terminal LPXTG motif, also characteristic of these proteins and is expected to anchor the protein to the peptidoglycan as seen in internalins structures such as InlA, InlI, InlJ or InlK [, ].The solved structure of InlK, revealed the classical LRR domain at its N-terminal, followed by three domains generating a structure that resembles a "bent arm", with a potential partner recognition domain localised at the "elbow"region. Domains D1 and D2 are potentially involved in binding to protein partners while D3 and D4 most probably serve as pedestals. Elbow and pedestal domains might act as platforms for binding partner molecules [ ]. InlK recruits the Major vault protein (MVP) in an interaction that allows L. monocytogenes to escape from autophagy [].This entry corresponds to a conserved Ig-like fold domain, also known as the inter-repeat region that follows the LRRs [ ], and corresponds to the elbow domain described in the InlK structure []. This domain and the LRRs are required and sufficient for attachment to host cells.
Short Name	InlI_Ig-like