Summary: Archaebacterial flagellin
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Archaebacterial flagellin Provide feedback
Archaeal motility occurs by the rotation of flagella that show similarity to bacterial type IV pili, including the multiflagellin nature of the flagellar filament, N-terminal sequence similarities, as well as the presence of homologous proteins in the two systems [2,3]. Similar to type IV pilins, archaeal flagellins are initially synthesised with a short leader peptide that is cleaved by a membrane-located peptidase [3,4]. The enzyme responsible for the removal of the this leader peptide is FlaK [4]. Archaeal flagella are composed of a number of distinct flagellin proteins, specified by genes in two separate operons (A and B) [6].
Literature references
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Gerl L, Sumper M; , J Biol Chem 1988;263:13246-13251.: Halobacterial flagellins are encoded by a multigene family. Characterization of five flagellin genes. PUBMED:3417656 EPMC:3417656
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Ng SY, Chaban B, Jarrell KF;, J Mol Microbiol Biotechnol. 2006;11:167-191.: Archaeal flagella, bacterial flagella and type IV pili: a comparison of genes and posttranslational modifications. PUBMED:16983194 EPMC:16983194
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Thomas NA, Bardy SL, Jarrell KF; , FEMS Microbiol Rev 2001;25:147-174.: The archaeal flagellum: a different kind of prokaryotic motility structure. PUBMED:11250034 EPMC:11250034
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Bardy SL, Ng SY, Jarrell KF;, J Mol Microbiol Biotechnol. 2004;7:41-51.: Recent advances in the structure and assembly of the archaeal flagellum. PUBMED:15170402 EPMC:15170402
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Bardy SL, Jarrell KF;, Mol Microbiol. 2003;50:1339-1347.: Cleavage of preflagellins by an aspartic acid signal peptidase is essential for flagellation in the archaeon Methanococcus voltae. PUBMED:14622420 EPMC:14622420
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Tarasov VY, Pyatibratov MG, Tang SL, Dyall-Smith M, Fedorov OV;, Mol Microbiol. 2000;35:69-78.: Role of flagellins from A and B loci in flagella formation of Halobacterium salinarum. PUBMED:10632878 EPMC:10632878
This tab holds annotation information from the InterPro database.
InterPro entry IPR002774
Archaeal motility occurs by the rotation of flagella that are different to bacterial flagella, but show similarity to bacterial type IV pili. These similarities include the multiflagellin nature of the flagellar filament, N-terminal sequence similarities, as well as the presence of homologous proteins in the two systems [ PUBMED:16983194 , PUBMED:11250034 ]. Also unlike bacterial flagellins but similar to type IV pilins, archaeal flagellins are initially synthesised with a short leader peptide that is cleaved by a membrane-located peptidase [ PUBMED:11250034 , PUBMED:15170402 ]. The enzyme responsible for the removal of the this leader peptide is FlaK [ PUBMED:14622420 ].
Archaeal flagella are composed of a number of distinct flagellin proteins, specified by genes in two separate operons (A and B) [ PUBMED:10632878 ].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Molecular function | structural molecule activity (GO:0005198) |
Biological process | archaeal or bacterial-type flagellum-dependent cell motility (GO:0097588) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan Pilus (CL0327), which has the following description:
This clan contains bacterial and archaeal systems involved in flagellar or twitching motility, adhesion, protein secretion, and DNA uptake, such as type II secretion system (T2SS), the type IV pilus or the competence pilus (Com) [4]. Pili proteins enable the transfer of plasmid between bacteria. The families in this clan adopt an alpha helical structure which is packed against a beta sheet [2-3].
The clan contains the following 15 members:
Arch_flagellin Bundlin ComP_DUS GspH PilA4 Pilin Pilin_GH Pilin_PilX PilJ_C PilM PilS T2SSG T2SSI T2SSJ TcpAAlignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
Seed (38) |
Full (684) |
Representative proteomes | UniProt (3954) |
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RP15 (91) |
RP35 (298) |
RP55 (700) |
RP75 (1312) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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Seed (38) |
Full (684) |
Representative proteomes | UniProt (3954) |
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RP15 (91) |
RP35 (298) |
RP55 (700) |
RP75 (1312) |
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Raw Stockholm | |||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
Seed source: | Enright A & COG3354 & COG3353 |
Previous IDs: | none |
Type: | Family |
Sequence Ontology: | SO:0100021 |
Author: |
Enright A |
Number in seed: | 38 |
Number in full: | 684 |
Average length of the domain: | 173.3 aa |
Average identity of full alignment: | 21 % |
Average coverage of the sequence by the domain: | 87.06 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 164 | ||||||||||||
Family (HMM) version: | 19 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Structures
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 Arch_flagellin domain has been found. There are 68 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 sequence.
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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.