Protein Family Models

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)

Date:

2024-10-16

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)

Date:

2024-10-16

catecholate siderophore receptor Fiu is involved in the active transport across the outer membrane of iron complexed with catecholate siderophores such as dihydroxybenzoylserine and dihydroxybenzoate

Date:

2019-07-25

This subfamily model encompasses a wide variety of TonB-dependent outer membrane siderophore receptors. It has no overlap with TonB receptors known to transport other substances, but is likely incomplete due to lack of characterizations. It is likely that genuine siderophore receptors will be identified which score below the noise cutoff to this model at which point the model should be updated.

Date:

2024-06-12

Porin involved in the uptake of iron complexed with catecholate siderophores (e.g. dihydroxybenzoylserine, dihydroxybenzoate) and beta lactam agents; Fiu interacts with TonB which provides the energy required for transport across the outer membrane; acts as a receptor for iron-siderophores and microcins E492, M, and H47; outer membrane protein

Date:

2021-08-26