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outer membrane beta-barrel protein
This family includes proteins annotated as TonB dependent receptors. But it is also likely to contain other membrane beta barrel proteins of other functions. (from Pfam)
TonB-dependent receptor plug domain-containing protein
The Plug domain has been shown to be an independently folding subunit of the TonB-dependent receptors ([1]). It acts as the channel gate, blocking the pore until the channel is bound by ligand. At this point it under goes conformational changes opens the channel. [1]. 15111112. The plug domain of a neisserial TonB-dependent transporter retains structural integrity in the absence of its transmembrane beta-barrel. Oke M, Sarra R, Ghirlando R, Farnaud S, Gorringe AR, Evans RW, Buchanan SK;. FEBS Lett 2004;564:294-300. (from Pfam)
TonB-dependent receptor domain-containing protein
This entry represents the beta-barrel domain of TonB-dependent receptors, such as BtuB, CirA, FatA, FcuT, FecA, FepA, among others [1]. [1]. 9886293. Crystal structure of the outer membrane active transporter FepA from Escherichia coli. Buchanan SK, Smith BS, Venkatramani L, Xia D, Esser L, Palnitkar M, Chakraborty R, van der Helm D, Deisenhofer J;. Nat Struct Biol 1999;6:56-63. (from Pfam)
TonB-dependent receptor plug domain-containing protein may act as a TonB-dependent siderophore receptor, a channel to allow import of iron-siderophore complexes; similar to Escherichia coli ferrienterobactin receptor, which is involved in the initial step of iron uptake by binding ferrienterobactin
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