Summary: Bacterial flagellin C-terminal helical region
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Bacterial flagellin C-terminal helical region Provide feedback
Flagellins polymerise to form bacterial flagella. There is some similarity between this family and PF00669 particularly the motif NRFXSXIXXL. It has been suggested that these two regions associate  and this is shown to be correct as structurally this family forms an extended helix that interacts with PF00700.
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR001029Bacterial flagella are responsible for motility and chemotaxis [PUBMED:2211662]. They comprise a basal body, a hook and a filament, the latter accounting for 98% of the mass [PUBMED:2498283]. Flagellin is the subunit protein that polymerises to form the flagellae [PUBMED:3536885], the subunits being transported through the centre of the filament to the tip, where they then polymerise [PUBMED:2211662]. Both the N- and C- termini of the subunit protein, which are alpha-helical in structure [PUBMED:2211662], are required to mediate polymerisation. Although no export or assembly consensus sequences have been identified, Ala, Val, Leu, Ile, Gly, Ser, Thr, Asn, Gln and Asp tend to make up around 90% of the sequence, Cys and Trp being absent [PUBMED:2498283].
This entry represents the N and C termini that come together to form the D0 and D1 structural domains [PUBMED:12904785]. These domains are responsible for flagellin's ability to polymerise into a filament.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||bacterial-type flagellum (GO:0009288)|
|Molecular function||structural molecule activity (GO:0005198)|
|Biological process||ciliary or flagellar motility (GO:0001539)|
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Curation and family details
|Seed source:||Pfam-B_41 (release 2.1)|
|Number in seed:||33|
|Number in full:||7466|
|Average length of the domain:||81.80 aa|
|Average identity of full alignment:||34 %|
|Average coverage of the sequence by the domain:||21.70 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||16|
|Download:||download the raw HMM for this family|
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There is 1 interaction 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 Flagellin_C domain has been found. There are 11 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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