Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
ATonB_dep_Rec_1e5fokA1 A: beta barrelsX: Outer membrane meander beta-barrelsH: PorinsT: Ligand-gated protein channelF: TonB_dep_Rec_1ECOD (1.6)
APluge5fokA2 A: a+b complex topologyX: N0 domain in phage tail proteins and secretins-likeH: TonB-dependent receptor plug domain (From Topology)T: TonB-dependent receptor plug domainF: PlugECOD (1.6)
BTonB_dep_Rec_1e5fokB2 A: beta barrelsX: Outer membrane meander beta-barrelsH: PorinsT: Ligand-gated protein channelF: TonB_dep_Rec_1ECOD (1.6)
BPluge5fokB1 A: a+b complex topologyX: N0 domain in phage tail proteins and secretins-likeH: TonB-dependent receptor plug domain (From Topology)T: TonB-dependent receptor plug domainF: PlugECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A2.170.130.10 Mainly Beta Beta Complex Ferric Hydroxamate Uptake Protein Chain A, domain 1CATH (4.3.0)
A2.40.170.20 Mainly Beta Beta Barrel Maltoporin Chain ACATH (4.3.0)
B2.170.130.10 Mainly Beta Beta Complex Ferric Hydroxamate Uptake Protein Chain A, domain 1CATH (4.3.0)
B2.40.170.20 Mainly Beta Beta Barrel Maltoporin Chain ACATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF00593TonB dependent receptor-like, beta-barrel (TonB_dep_Rec_b-barrel)TonB dependent receptor-like, beta-barrelThis entry represents the beta-barrel domain of TonB-dependent receptors, such as BtuB, CirA, FatA, FcuT, FecA, FepA, among others [1].Domain
A, B
PF07715TonB-dependent Receptor Plug Domain (Plug)TonB-dependent Receptor Plug DomainThe 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

Membrane Protein Annotation: PDBTM PDBTM Database Homepage

Membrane Protein Annotation: MemProtMD MemProtMD Database Homepage