Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad1nqea_ Membrane and cell surface proteins and peptides Transmembrane beta-barrels Porins Ligand-gated protein channel Outer membrane cobalamin transporter BtuB (Escherichia coli ) [TaxId: 562 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyPorins 8042029 3000224 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
ATonB_dep_Rece1nqeA1 A: beta barrelsX: Outer membrane meander beta-barrelsH: PorinsT: Ligand-gated protein channelF: TonB_dep_RecECOD (1.6)
APluge1nqeA2 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)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
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
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