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Flagellin-like structural proteins are found in other portions of the flagellum, such as the hook (flgE; ), the rod at the base, and the cap at the top. [ 7 ] The middle part of E. coli (and related) flagellin, D3, displays a beta-folium fold and appears to maintain flagellar stability.
The bacterial flagellum is made up of protein subunits of flagellin. [12] Its shape is a 20-nanometer-thick hollow tube. It is helical and has a sharp bend just outside the outer membrane; this "hook" allows the axis of the helix to point directly away from the cell.
Flagellin is also another PAMP that is recognized via the constant domain, D1 by TLR5. [7] Despite being a protein, its N- and C-terminal ends are highly conserved, due to its necessity for function of flagella. [8]
Toll-like receptor 5, also known as TLR5, is a protein which in humans is encoded by the TLR5 gene. [5] It is a member of the toll-like receptor (TLR) family. TLR5 is known to recognize bacterial flagellin from invading mobile bacteria. [6]
The microbe-specific molecules that are recognized by a given PRR are called pathogen-associated molecular patterns (PAMPs) and include bacterial carbohydrates (such as lipopolysaccharide or LPS, mannose), nucleic acids (such as bacterial or viral DNA or RNA), bacterial peptides (flagellin, microtubule elongation factors), peptidoglycans and ...
In biology, phase variation is a method for dealing with rapidly varying environments without requiring random mutation. It involves the variation of protein expression, frequently in an on-off fashion, within different parts of a bacterial population.
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Similarly, flagella grow by exporting flagellin through the flagellar machinery. It is hypothesised that the flagellum evolved from the type three secretory system. It is hypothesised that the flagellum evolved from the type three secretory system.