| Description | This entry includes flagellar M-ring protein (FliF) and Yop proteins translocation lipoprotein J (YscJ). They share a low level of similarity, presumably due to evolution of the type III secretion system from the flagellar biosynthetic pathway.FliF is the major protein of the M-ring in bacterial flagellar basal body [].The basal body consists of four rings (L,P,S and M) surrounding the flagellar rod, which is believed to transmit motor rotation to the filament [ ]. The M ring is integral to the inner membrane of the cell, and may be connected to the rod via the S (supramembrane) ring, which lies just distalto it. The L and P rings reside in the outer membrane and periplasmic space, respectively.FliF lacks a signal peptide and is predicted to have considerable α-helical structure, including an N-terminal sequence that is likelyto be membrane-spanning [ ]. Overall, however, FliF has a relativelyhydrophilic sequence, with a high charge density, especially towards its C terminus [].The type III secretion system is of great interest as it is used to transport virulence factors from the pathogen directly into the host cell [] and is only triggered when the bacterium comes into close contact with the host. The protein subunits of the system are very similar to those of bacterial flagellar biosynthesis []. However, while the latter forms a ring structure to allow secretion of flagellin and is an integral part of the flagellum itself, type III subunits in the outer membrane translocate secreted proteins through a channel-like structure.One of the outer membrane protein subunit families, termed "K"here for nomenclature purposes, aids in the structural assembly of the invasion complex [ ]. It is also described as a lipoprotein. These lipoproteins include the PrgK and SsaJ from Salmonella, MxiJ from Shigella, YscJ from Yersinia, and from the plant enteropathogens NolT (Rhizobium) and HrcJ (Erwinia). | Name | Lipoprotein YscJ/Flagellar M-ring protein |
| Short Name | YscJ/FliF | Type | Family |
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