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The filament is made up of eleven smaller "protofilaments", nine of which contains flagellin in the L-type shape and the other two in the R-type shape. [6] The helical N-and C-termini of flagellin form the inner core of the flagellin protein, and is responsible for flagellin's ability to polymerize into a filament. The middle residues make up ...
A flagellum (/ f l ə ˈ dʒ ɛ l əm /; pl.: flagella) (Latin for 'whip' or 'scourge') is a hair-like appendage that protrudes from certain plant and animal sperm cells, from fungal spores (), and from a wide range of microorganisms to provide motility.
FLS2 consists of 3 domains: an extracellular, a transmembrane, and an intracellular. The extracellular domain is known as the Leucine-rich repeat (LRR) domain. It is in this region, which is the amino-terminus, where it is said to have direct interaction with flagellin initiating the response of FLS2 to flg22.
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.
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 ]
7100 53791 Ensembl ENSG00000187554 ENSMUSG00000079164 UniProt O60602 Q9JLF7 RefSeq (mRNA) NM_003268 NM_016928 RefSeq (protein) NP_003259 NP_058624 Location (UCSC) Chr 1: 223.11 – 223.14 Mb Chr 1: 182.78 – 182.8 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Toll-like receptor 5, also known as TLR5, is a protein which in humans is encoded by the TLR5 gene. It is a member of the ...
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.
Like EFR, FLS2 (flagellin-sensing 2) is a plant receptor-like kinase that acts as a PRR in the plant innate immune system. [10] [12] Instead of binding to EF-Tu, it binds to flagellin, another highly conserved structure present on many pathogens. Flagellin, like EF-Tu, is a good target for the plant immune system since it is so widespread.