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The FrpB iron transporter from Neisseria meningitidis (F3-3 variant) External Resource: Annotation Chains Family Name Domain Identifier Architecture Possible Homology Homology Topology Family Provenance Source (Version) A TonB_dep_Rec_1 e4aipA1 A: beta barrels X: Outer membrane meander beta-barrels H: Porins T: Ligand-gated protein channel F: TonB_dep_Rec_1 ECOD (1.6) A Plug e4aipA2 A: a+b complex topology X: N0 domain in phage tail proteins and secretins-like H: TonB-dependent receptor plug domain (From Topology) T: TonB-dependent receptor plug domain F: Plug ECOD (1.6) B TonB_dep_Rec_1 e4aipB1 A: beta barrels X: Outer membrane meander beta-barrels H: Porins T: Ligand-gated protein channel F: TonB_dep_Rec_1 ECOD (1.6) B Plug e4aipB2 A: a+b complex topology X: N0 domain in phage tail proteins and secretins-like H: TonB-dependent receptor plug domain (From Topology) T: TonB-dependent receptor plug domain F: Plug ECOD (1.6) C TonB_dep_Rec_1 e4aipC1 A: beta barrels X: Outer membrane meander beta-barrels H: Porins T: Ligand-gated protein channel F: TonB_dep_Rec_1 ECOD (1.6) C Plug e4aipC2 A: a+b complex topology X: N0 domain in phage tail proteins and secretins-like H: TonB-dependent receptor plug domain (From Topology) T: TonB-dependent receptor plug domain F: Plug ECOD (1.6)
Chains Accession Name Description Comments Source PF00593 TonB dependent receptor-like, beta-barrel (TonB_dep_Rec_b-barrel) TonB dependent receptor-like, beta-barrel This entry represents the beta-barrel domain of TonB-dependent receptors, such as BtuB, CirA, FatA, FcuT, FecA, FepA, among others [1]. Domain PF07715 TonB-dependent Receptor Plug Domain (Plug) TonB-dependent Receptor Plug Domain 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 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. Domain
Chains Polymer Molecular Function Biological Process Cellular Component FE-REGULATED PROTEIN B -
