Summary
FliG C-terminal domain
FliG is a component of the flageller rotor, present in about 25 copies per flagellum. This domain functions specifically in motor rotation.
Literature references
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Lloyd SA, Whitby FG, Blair DF, Hill CP; , Nature 1999;400:472-475.: Structure of the C-terminal domain of FliG, a component of the rotor in the bacterial flagellar motor [In Process Citation] PUBMED:10440379
InterPro entry IPR000090
The flagellar motor switch in Escherichia coli and Salmonella typhimurium regulates the direction of flagellar rotation and hence controls swimming behaviour PUBMED:8224881. The switch is a complex apparatus that responds to signals transduced by the chemotaxis sensory signalling system during chemotactic behaviour PUBMED:8224881. CheY, the chemotaxis response regulator, is believed to act directly on the switch to induce tumbles in the swimming pattern, but no physical interactions of CheY and switch proteins have yet been demonstrated.
The switch complex comprises at least three proteins - FliG, FliM and FliN. It has been shown that FliG interacts with FliM, FliM interacts with itself, and FliM interacts with FliN PUBMED:8631704. Several residues within the middle third of FliG appear to be strongly involved in the FliG-FliM interaction, with residues near the N- or C-termini being less important PUBMED:8631704. Such clustering suggests that FliG-FliM interaction plays a central role in switching.
Analysis of the FliG, FliM and FliN sequences shows that none are especially hydrophobic or appear to be integral membrane proteins PUBMED:2656645. This result is consistent with other evidence suggesting that the proteins may be peripheral to the membrane, possibly mounted on the basal body M ring PUBMED:2656645, PUBMED:1631122. FliG is present in about 25 copies per flagellum. This structure of the C-terminal domain is known, this domain functions specifically in motor rotation PUBMED:10440379.
Clan
This family is a member of clan FliG (CL0436), which contains the following 2 members:
FliG_C MgtE_NGene Ontology
| Cellular component | flagellin-based flagellum (GO:0009288) |
| Molecular function | motor activity (GO:0003774) |
| Biological process | ciliary or flagellar motility (GO:0001539) |
| chemotaxis (GO:0006935) |
Internal database links
| SCOOP: | MgtE_N MR_MLE_N MgtE |
External database links
| PANDIT: | PF01706 |
| SCOP: | 1qc7 |
| SYSTERS: | FliG_C |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...
View options
Formatting options
Download options
Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.
You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER2.
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. 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 or full alignments.
Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.
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: | [1] |
| Previous IDs: | FliG-C; |
| Type: | Domain |
| Author: | Bateman A |
| Number in seed: | 154 |
| Number in full: | 940 |
| Average length of the domain: | 110.00 aa |
| Average identity of full alignment: | 37 % |
| Average coverage of the sequence by the domain: | 32.28 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
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| Model details: |
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| Model length: | 110 | ||||||||||||
| Family (HMM) version: | 9 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
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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 FliG_C domain has been found.
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