Summary: Membrane-attachment and polymerisation-promoting switch
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|Cell division protein FtsA|
E. coli cells producing FtsA-GFP, which localizes to the cell division site.
|Chromosome||Genome: 0.1 - 0.11 Mb|
|SHS2 "1C" domain inserted in FtsA|
Along with other bacterial actin homologs such as MreB, ParM, and MamK, these proteins suggest that eukaryotic actin has a common ancestry. Like the other bacterial actins, FtsA binds ATP and can form actin-like filaments. The FtsA-FtsA interface has been defined by structural as well as genetic analysis. Although present in many diverse Gram-positive and Gram-negative species, FtsA is absent in actinobacteria and cyanobacteria. FtsA also is structurally similar to PilM, a type IV pilus ATPase.
FtsA is required for proper cytokinesis in bacteria such as Escherichia coli, Caulobacter crescentus, and Bacillus subtilis. Originally isolated in a screen for E. coli cells that could divide at 30ËšC but not at 40ËšC, FtsA stands for "filamentous temperature sensitive A". Many thermosensitive alleles of E. coli ftsA exist, and all map in or near the ATP binding pocket. Suppressors that restore normal function map either to the binding pocket or to the FtsA-FtsA interface.
FtsA localizes to the cytokinetic ring formed by FtsZ (Z ring). One of FtsA's functions in cytokinesis is to tether FtsZ polymers to the cytoplasmic membrane via a conserved C-terminal amphipathic helix, forming an "A ring" in the process. Another essential division protein, ZipA, also tethers the Z ring to the membrane and exhibits overlapping function with FtsA. FtsZ, FtsA and ZipA together are called the proto-ring because they are involved in a specific initial phase of cytokinesis. Removal of this helix results in the formation of very long and stable polymer bundles of FtsA in the cell that do not function in cytokinesis. Another subdomain of FtsA (2B) is required for interactions with FtsZ, via the conserved C-terminus of FtsZ. Other FtsZ regulators including MinC and ZipA bind to the same C terminus of FtsZ. Finally, subdomain 1C, which is in a unique position relative to MreB and actin, is required for FtsA to recruit downstream cell division proteins such as FtsN.
Although FtsA is essential for viability in E. coli, it can be deleted in B. subtilis. B. subtilis cells lacking FtsA divide poorly, but still survive. Another FtsZ-interacting protein, SepF (originally named YlmF; ), is able to replace FtsA in B. subtilis, suggesting that SepF and FtsA have overlapping functions.
An allele of FtsA called FtsA* (R286W) is able to bypass the normal requirement for the ZipA in E. coli cytokinesis. FtsA* also causes cells to divide at a shorter cell length than normal, suggesting that FtsA may normally receive signals from the septum synthesis machinery to regulate when cytokinesis can proceed. Other FtsA*-like alleles have been found, and they mostly decrease FtsA-FtsA interactions. Oligomeric state of FtsA is likely important for regulating its activity, its ability to recruit the later cell division proteins  and its ability to bind ATP. Other cell division proteins of E. coli, including FtsN and the ABC transporter homologs FtsEX, seem to regulate septum constriction by signaling through FtsA, and the FtsQLB subcomplex is also involved in promoting FtsN-mediated septal constriction.
FtsA binds directly to the conserved C-terminal domain of FtsZ. This FtsA-FtsZ interaction is likely involved in regulating FtsZ polymer dynamics. In vitro, E. coli FtsA disassembles FtsZ polymers in the presence of ATP, both in solution, as FtsA*  and on supported lipid bilayers. E. coli FtsA itself does not assemble into detectable structures except when on membranes, where it forms dodecameric minirings that often pack in clusters and bind to single FtsZ protofilaments. In contrast, FtsA* forms arcs on lipid membranes but rarely closed minirings, supporting genetic evidence that this mutant has a weaker FtsA-FtsA interface. FtsA from Streptococcus pneumoniae forms helical filaments in the presence of ATP, but no interactions with FtsZ have been reported yet. FtsA from Staphylococcus aureus forms actin-like filaments similar to those of FtsA from Thermotoga maritima. In addition, S. aureus FtsA enhances the GTPase activity of FtsZ. In a liposome system, FtsA* stimulates FtsZ to form rings that can divide liposomes, mimicking cytokinesis in vitro.
- van den Ent F, LÃ¶we J (Oct 2000). "Crystal structure of the cell division protein FtsA from Thermotoga maritima". The EMBO Journal. 19 (20): 5300â€“7. doi:10.1093/emboj/19.20.5300. PMC 313995. PMID 11032797.
- Gunning PW, Ghoshdastider U, Whitaker S, Popp D, Robinson RC (Jun 2015). "The evolution of compositionally and functionally distinct actin filaments". Journal of Cell Science. 128 (11): 2009â€“19. doi:10.1242/jcs.165563. PMID 25788699.
- Ghoshdastider U, Jiang S, Popp D, Robinson RC (Jul 2015). "In search of the primordial actin filament". Proceedings of the National Academy of Sciences of the United States of America. 112 (30): 9150â€“1. doi:10.1073/pnas.1511568112. PMC 4522752. PMID 26178194.
- Szwedziak P, Wang Q, Freund SM, LÃ¶we J (May 2012). "FtsA forms actin-like protofilaments". The EMBO Journal. 31 (10): 2249â€“60. doi:10.1038/emboj.2012.76. PMC 3364754. PMID 22473211.
- Pichoff S, Shen B, Sullivan B, Lutkenhaus J (Jan 2012). "FtsA mutants impaired for self-interaction bypass ZipA suggesting a model in which FtsA's self-interaction competes with its ability to recruit downstream division proteins". Molecular Microbiology. 83 (1): 151â€“67. doi:10.1111/j.1365-2958.2011.07923.x. PMC 3245357. PMID 22111832.
- Karuppiah V, Derrick JP (Jul 2011). "Structure of the PilM-PilN inner membrane type IV pilus biogenesis complex from Thermus thermophilus". The Journal of Biological Chemistry. 286 (27): 24434â€“42. doi:10.1074/jbc.M111.243535. PMC 3129222. PMID 21596754.
- Kohiyama M, Cousin D, Ryter A, Jacob F (April 1966). "Mutants thermosensibles d'Escherichia coli K12". Annales de l'Institute Pasteur. 110 (4): 465â€“86.
- Herricks JR, Nguyen D, Margolin W (Nov 2014). "A thermosensitive defect in the ATP binding pocket of FtsA can be suppressed by allosteric changes in the dimer interface". Molecular Microbiology. 94 (3): 713â€“27. doi:10.1111/mmi.12790. PMC 4213309. PMID 25213228.
- Pichoff S, Lutkenhaus J (Mar 2005). "Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA". Molecular Microbiology. 55 (6): 1722â€“34. doi:10.1111/j.1365-2958.2005.04522.x. PMID 15752196.
- Rico AI, Krupka M, Vicente M (Jul 2013). "In the beginning, Escherichia coli assembled the proto-ring: an initial phase of division". The Journal of Biological Chemistry. 288 (29): 20830â€“6. doi:10.1074/jbc.R113.479519. PMC 3774354. PMID 23740256.
- Rico AI, GarcÃa-Ovalle M, Mingorance J, Vicente M (Sep 2004). "Role of two essential domains of Escherichia coli FtsA in localization and progression of the division ring". Molecular Microbiology. 53 (5): 1359â€“71. doi:10.1111/j.1365-2958.2004.04245.x. PMID 15387815.
- Busiek KK, Eraso JM, Wang Y, Margolin W (Apr 2012). "The early divisome protein FtsA interacts directly through its 1c subdomain with the cytoplasmic domain of the late divisome protein FtsN". Journal of Bacteriology. 194 (8): 1989â€“2000. doi:10.1128/JB.06683-11. PMC 3318488. PMID 22328664.
- Ishikawa S, Kawai Y, Hiramatsu K, Kuwano M, Ogasawara N (Jun 2006). "A new FtsZ-interacting protein, YlmF, complements the activity of FtsA during progression of cell division in Bacillus subtilis". Molecular Microbiology. 60 (6): 1364â€“80. doi:10.1111/j.1365-2958.2006.05184.x. PMID 16796675.
- Geissler B, Elraheb D, Margolin W (Apr 2003). "A gain-of-function mutation in ftsA bypasses the requirement for the essential cell division gene zipA in Escherichia coli". Proceedings of the National Academy of Sciences of the United States of America. 100 (7): 4197â€“202. doi:10.1073/pnas.0635003100. PMC 153070. PMID 12634424.
- Geissler B, Shiomi D, Margolin W (Mar 2007). "The ftsA* gain-of-function allele of Escherichia coli and its effects on the stability and dynamics of the Z ring". Microbiology. 153 (Pt 3): 814â€“25. doi:10.1099/mic.0.2006/001834-0. PMC 4757590. PMID 17322202.
- Du S, Pichoff S, Lutkenhaus J (Aug 2016). "FtsEX acts on FtsA to regulate divisome assembly and activity". Proc Natl Acad Sci USA. 113 (34): 5052â€“5061. doi:10.1073/pnas.1606656113. PMC 5003251. PMID 27503875.
- Pichoff S, Du S, Lutkenhaus J (Mar 2015). "The bypass of ZipA by overexpression of FtsN requires a previously unknown conserved FtsN motif essential for FtsA-FtsN interaction supporting a model in which FtsA monomers recruit late cell division proteins to the Z ring". Molecular Microbiology. 95 (6): 971â€“987. doi:10.1111/mmi.12907. PMC 4364298. PMID 25496259.
- Tsang MJ, Bernhardt TG (Mar 2015). "A role for the FtsQLB complex in cytokinetic ring activation revealed by an ftsL allele that accelerates division". Molecular Microbiology. 95 (6): 924â€“944. doi:10.1111/mmi.12905. PMC 4414402. PMID 25496050.
- Liu B, Persons L, Lee L, de Boer P (Mar 2015). "Roles for both FtsA and the FtsBLQ subcomplex in FtsN-stimulated cell constriction in Escherichia coli". Molecular Microbiology. 95 (6): 945â€“970. doi:10.1111/mmi.12906. PMC 4428282. PMID 25496160.
- Pichoff S, Lutkenhaus J (2002). "Unique and overlapping roles for ZipA and FtsA in septal ring assembly in Escherichia coli". EMBO Journal. 21 (4): 685â€“93. doi:10.1093/emboj/21.4.685. PMC 125861. PMID 11847116.
- Beuria TK, Mullapudi S, Mileykovskaya E, Sadasivam M, Dowhan W, Margolin W (May 2009). "Adenine nucleotide-dependent regulation of assembly of bacterial tubulin-like FtsZ by a hypermorph of bacterial actin-like FtsA". The Journal of Biological Chemistry. 284 (21): 14079â€“86. doi:10.1074/jbc.M808872200. PMC 2682856. PMID 19297332.
- Loose M, Mitchison TJ (Jan 2014). "The bacterial cell division proteins FtsA and FtsZ self-organize into dynamic cytoskeletal patterns". Nature Cell Biology. 16 (1): 38â€“46. doi:10.1038/ncb2885. PMC 4019675. PMID 24316672.
- Krupka, Marcin; Rowlett, Veronica W.; Morado, Dustin; Vitrac, Heidi; Schoenemann, Kara; Liu, Jun; Margolin, William (2017-07-11). "Escherichia coli FtsA forms lipid-bound minirings that antagonize lateral interactions between FtsZ protofilaments". Nature Communications. 8: 15957. doi:10.1038/ncomms15957. ISSN 2041-1723. PMC 5508204. PMID 28695917.
- Lara B, Rico AI, Petruzzelli S, Santona A, Dumas J, Biton J, Vicente M, Mingorance J, Massidda O (2005). "Cell division in cocci: localization and properties of the Streptococcus pneumoniae FtsA protein" (PDF). Molecular Microbiology. 55 (3): 699â€“711. doi:10.1111/j.1365-2958.2004.04432.x. PMID 15660997.
- Fujita J, Maeda Y, Nagao C, Tsuchiya Y, Miyazaki Y, Hirose M, Mizohata E, Matsumoto Y, Inoue T, Mizuguchi K, Matsumura H (May 2014). "Crystal structure of FtsA from Staphylococcus aureus". FEBS Letters. 588 (10): 1879â€“85. doi:10.1016/j.febslet.2014.04.008. PMID 24746687.
- Osawa M, Erickson HP (2013). "Liposome division by a simple bacterial division machinery". Proceedings of the National Academy of Sciences of the United States of America. 110 (27): 11000â€“4. doi:10.1073/pnas.1222254110. PMC 3703997. PMID 23776220.
- Anantharaman, V; Aravind, L (1 September 2004). "The SHS2 module is a common structural theme in functionally diverse protein groups, like Rpb7p, FtsA, GyrI, and MTH1598/TM1083 superfamilies". Proteins. 56 (4): 795â€“807. doi:10.1002/prot.20140. PMID 15281131.
"DUF" families are annotated with the Domain of unknown function Wikipedia article. This is a general article, with no specific information about individual Pfam DUFs. If you have information about this particular DUF, please let us know using the "Add annotation" button below.
Membrane-attachment and polymerisation-promoting switch Provide feedback
This family is the C-terminal region of essential streptococcal FtsA proteins and their homologues. It acts as an intra-molecular switch, triggered by ATP, to promote polymerisation of the whole protein and to attach it to the membrane. FtsA is essential for the formation of the septum that divides fully-grown cells into two daughter cells at cell-division. FtsA anchors the constricting FtsZ ring to the membrane .
This tab holds annotation information from the InterPro database.
InterPro entry IPR021873
FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains [PUBMED:9352931].
This C-terminal domain is found in FtsA from Firmicutes (Gram-positive bacteria). It acts as an intra-molecular switch, triggered by ATP, to promote polymerisation of the whole protein and to attach it to the membrane [PUBMED:25425238].
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
The graphic that is shown by default represents the longest sequence with a given architecture. Each row contains the following information:
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a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
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EGFdomains, and finally a single
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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, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...
There are various ways to view or download the sequence alignments that we store. We provide several sequence viewers and a plain-text Stockholm-format file for download.
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the UniProtKB sequence database using the family HMM
- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
You can see the alignments as HTML or in three different sequence viewers:
- a Java applet developed at the University of Dundee. You will need Java installed before running jalview
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You can download (or view in your browser) a text representation of a Pfam alignment in various formats:
You can also change the order in which sequences are listed in the alignment, change how insertions are represented, alter the characters that are used to represent gaps in sequences and, finally, choose whether to download the alignment or to view it in your browser directly.
You may find that large alignments cause problems for the viewers and the reformatting tool, so we also provide all alignments in Stockholm format. You can download either the plain text alignment, or a gzipped version of it.
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.
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
Format an alignment
We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
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...
If you find these logos useful in your own work, please consider citing the following article:
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.
|Seed source:||PFAM-B_3216 (release 23.0)|
|Author:||Assefa S , Coggill P , Bateman A|
|Number in seed:||19|
|Number in full:||115|
|Average length of the domain:||72.30 aa|
|Average identity of full alignment:||25 %|
|Average coverage of the sequence by the domain:||16.34 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||9|
|Download:||download the raw HMM for this family|
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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the More....
This chart is a modified "sunburst" visualisation of the species tree for this family. It shows each node in the tree as a separate arc, arranged radially with the superkingdoms at the centre and the species arrayed around the outermost ring.
How the sunburst is generated
The tree is built by considering the taxonomic lineage of each sequence that has a match to this family. For each node in the resulting tree, we draw an arc in the sunburst. The radius of the arc, its distance from the root node at the centre of the sunburst, shows the taxonomic level ("superkingdom", "kingdom", etc). The length of the arc represents either the number of sequences represented at a given level, or the number of species that are found beneath the node in the tree. The weighting scheme can be changed using the sunburst controls.
In order to reduce the complexity of the representation, we reduce the number of taxonomic levels that we show. We consider only the following eight major taxonomic levels:
Colouring and labels
Segments of the tree are coloured approximately according to their superkingdom. For example, archeal branches are coloured with shades of orange, eukaryotes in shades of purple, etc. The colour assignments are shown under the sunburst controls. Where space allows, the name of the taxonomic level will be written on the arc itself.
As you move your mouse across the sunburst, the current node will be highlighted. In the top section of the controls panel we show a summary of the lineage of the currently highlighed node. If you pause over an arc, a tooltip will be shown, giving the name of the taxonomic level in the title and a summary of the number of sequences and species below that node in the tree.
Anomalies in the taxonomy tree
There are some situations that the sunburst tree cannot easily handle and for which we have work-arounds in place.
Missing taxonomic levels
Some species in the taxonomic tree may not have one or more of the main eight levels that we display. For example, Bos taurus is not assigned an order in the NCBI taxonomic tree. In such cases we mark the omitted level with, for example, "No order", in both the tooltip and the lineage summary.
Unmapped species names
The tree is built by looking at each sequence in the full alignment for the family. We take the name of the species given by UniProt and try to map that to the full taxonomic tree from NCBI. In some cases, the name chosen by UniProt does not map to any node in the NCBI tree, perhaps because the chosen name is listed as a synonym or a misspelling in the NCBI taxonomy.
So that these nodes are not simply omitted from the sunburst tree, we group them together in a separate branch (or segment of the sunburst tree). Since we cannot determine the lineage for these unmapped species, we show all levels between the superkingdom and the species as "uncategorised".
Since we reduce the species tree to only the eight main taxonomic levels, sequences that are mapped to the sub-species level in the tree would not normally be shown. Rather than leave out these species, we map them instead to their parent species. So, for example, for sequences belonging to one of the Vibrio cholerae sub-species in the NCBI taxonomy, we show them instead as belonging to the species Vibrio cholerae.
Too many species/sequences
For large species trees, you may see blank regions in the outer layers of the sunburst. These occur when there are large numbers of arcs to be drawn in a small space. If an arc is less than approximately one pixel wide, it will not be drawn and the space will be left blank. You may still be able to get some information about the species in that region by moving your mouse across the area, but since each arc will be very small, it will be difficult to accurately locate a particular species.
The tree shows the occurrence of this domain across different species. More...
We show the species tree in one of two ways. For smaller trees we try to show an interactive representation, which allows you to select specific nodes in the tree and view them as an alignment or as a set of Pfam domain graphics.
Unfortunately we have found that there are problems viewing the interactive tree when the it becomes larger than a certain limit. Furthermore, we have found that Internet Explorer can become unresponsive when viewing some trees, regardless of their size. We therefore show a text representation of the species tree when the size is above a certain limit or if you are using Internet Explorer to view the site.
If you are using IE you can still load the interactive tree by clicking the "Generate interactive tree" button, but please be aware of the potential problems that the interactive species tree can cause.
For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.
We also count the number of unique sequences on which each domain is found, which is shown in green. Note that a domain may appear multiple times on the same sequence, leading to the difference between these two numbers.
Finally, we group sequences from the same organism according to the NCBI code that is assigned by UniProt, allowing us to count the number of distinct sequences on which the domain is found. This value is shown in the pink boxes.
We use the NCBI species tree to group organisms according to their taxonomy and this forms the structure of the displayed tree. Note that in some cases the trees are too large (have too many nodes) to allow us to build an interactive tree, but in most cases you can still view the tree in a plain text, non-interactive representation. Those species which are represented in the seed alignment for this domain are highlighted.
You can use the tree controls to manipulate how the interactive tree is displayed:
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Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.