Summary: TonB-dependent Receptor Plug Domain
This is the Wikipedia entry entitled "TonB-dependent receptor plug domain". More...
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TonB-dependent receptor plug domain Edit Wikipedia article
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TonB-dependent Receptor Plug Domain Provide feedback
The Plug domain has been shown to be an independently folding subunit of the TonB-dependent receptors (). 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.
Oke M, Sarra R, Ghirlando R, Farnaud S, Gorringe AR, Evans RW, Buchanan SK; , FEBS Lett 2004;564:294-300.: The plug domain of a neisserial TonB-dependent transporter retains structural integrity in the absence of its transmembrane beta-barrel. PUBMED:15111112 EPMC:15111112
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR012910
In Escherichia coli the TonB protein interacts with outer membrane receptor proteins that carry out high-affinity binding and energy-dependent uptake of specific substrates into the periplasmic space [PUBMED:14499604]. These substrates are either poorly permeable through the porin channels or are encountered at very low concentrations. In the absence of TonB, these receptors bind their substrates but do not carry out active transport. TonB-dependent regulatory systems consist of six components: a specialised outer membrane-localized TonB-dependent receptor (TonB-dependent transducer) that interacts with its energizing TonB-ExbBD protein complex, a cytoplasmic membrane-localized anti-sigma factor and an extracytoplasmic function (ECF)-subfamily sigma factor [PUBMED:15993072]. The TonB complex senses signals from outside the bacterial cell and transmits them via two membranes into the cytoplasm, leading to transcriptional activation of target genes. The proteins that are currently known or presumed to interact with TonB include BtuB [PUBMED:12652322], CirA, FatA, FcuT, FecA [PUBMED:11872840], FhuA [PUBMED:9865695], FhuE, FepA [PUBMED:9886293], FptA, HemR, IrgA, IutA, PfeA, PupA and Tbp1. The TonB protein also interacts with some colicins. Most of these proteins contain a short conserved region at their N terminus [PUBMED:12957833].
This entry represents the plug domain, which has been shown to be an independently folding subunit of the TonB-dependent receptors [PUBMED:15111112]. It acts as the channel gate, blocking the pore until the channel is bound by a ligand. At this point it undergoes conformational changes and opens the channel.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||membrane (GO:0016020)|
|Molecular function||receptor activity (GO:0004872)|
|Biological process||transport (GO:0006810)|
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Curation and family details
|Seed source:||Yeats C|
|Number in seed:||635|
|Number in full:||24391|
|Average length of the domain:||109.90 aa|
|Average identity of full alignment:||21 %|
|Average coverage of the sequence by the domain:||12.94 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 17690987 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||13|
|Download:||download the raw HMM for this family|
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There are 7 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Plug domain has been found. There are 78 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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