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<h1 id="firstHeading" class="firstHeading mw-first-heading"><span class="mw-page-title-main">FtsA</span></h1>
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<div id="mw-content-text" class="mw-body-content mw-content-ltr" lang="de" dir="ltr"><div class="mw-content-ltr mw-parser-output" lang="de" dir="ltr"><table class="wikitable hintergrundfarbe-basis infobox float-right" id="Vorlage_Infobox_Protein_FtsA" style="font-size:90%; margin-top:0; width:350px;" summary="Infobox Protein">
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<th colspan="3" style="background:#90EE90; color:#202122;">FtsA
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<td colspan="3"><span typeof="mw:File"></span>
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<td colspan="3" class="hintergrundfarbe1" style="text-align:center; font-size:smaller; font-weight:bold;">nach <a href="Protein_Data_Bank" title="Protein Data Bank">PDB</a> <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/1e4g">1e4g</a>
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<td colspan="3" class="hintergrundfarbe1" style="font-size:smaller;">
<p>Vorhandene Strukturdaten: <span class=""><a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/1e4g">1e4g</a></span>, <span class=""><a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/1e4f">1e4f</a></span>
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<td><a href="Molare_Masse" title="Molare Masse">Masse</a>/Länge <a href="Prim%C3%A4rstruktur" title="Primärstruktur">Primärstruktur</a>
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<td colspan="2" style="text-align:center;">45.330 <a href="Atomare_Masseneinheit" title="Atomare Masseneinheit">Dalton</a> / 420 <a href="Aminos%C3%A4ure" class="mw-redirect" title="Aminosäure">Aminosäuren</a>
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<th colspan="3" style="background:#90EE90; color:#202122;">Bezeichner
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<td>Externe IDs
</td>
<td colspan="2" class="">
<ul><li><a href="UniProt" title="UniProt">UniProt</a> <a rel="nofollow" class="external text" href="https://www.uniprot.org/uniprotkb/P0ABH0">P0ABH0</a></li></ul>
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<th colspan="3" style="background:#90EE90; color:#202122;">Enzymklassifikation
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<td><a href="EC-Nummer" title="EC-Nummer">EC, Kategorie</a>
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<td colspan="2" class="" style="text-align:center;">, <a href="ATPase" class="mw-redirect" title="ATPase">ATPase</a>
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<td>Substrat
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<td colspan="2" style="text-align:center;">Adenosintriphosphat
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<td>Produkte
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<td colspan="2" style="text-align:center;">Adenosindiphosphat und Phosphat
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<th colspan="3" style="background:#90EE90; color:#202122;">Vorkommen
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<td style="background:#C3FDB8; color:#202122;">Homologie-Familie
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<td colspan="2" style="text-align:center;"><a rel="nofollow" class="external text" href="http://hogenom.univ-lyon1.fr/query_sequence?seq=P0ABH0">Hovergen</a>
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</p><p><b>FtsA</b> (von <span style="font-style:normal;font-weight:normal"><a href="Englische_Sprache" title="Englische Sprache">englisch</a></span> <span lang="en-Latn" style="font-style:italic"><i>filamentous temperature sensitive A</i></span> ‚filamentös temperaturempfindlich A‘) ist ein <a href="Protein" title="Protein">Protein</a> des <a href="Zytoskelett" class="mw-redirect" title="Zytoskelett">Zytoskeletts</a> von <a href="Bakterien" title="Bakterien">Bakterien</a>, mit Ausnahme von <a href="Actinobakterien" class="mw-redirect" title="Actinobakterien">Actinobakterien</a> und <a href="Cyanobakterien" title="Cyanobakterien">Cyanobakterien</a>.
</p>
<div class="mw-heading mw-heading2"><h2 id="Eigenschaften">Eigenschaften</h2></div>
<p>FtsA dient in Bakterien zur Stabilisierung der <a href="Zelle_(Biologie)" title="Zelle (Biologie)">Zelle</a> und zur Fortbewegung (<a href="Motilit%C3%A4t" title="Motilität">Zellmotilität</a>), möglicherweise ist es an der Einleitung der <a href="Zellteilung" title="Zellteilung">Zellteilung</a> beteiligt.<sup id="cite_ref-pmid17322202”_1-0" class="reference"><a href="#cite_note-pmid17322202”-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup> FtsA ist ein <a href="Homologie_(Genetik)" title="Homologie (Genetik)">Homolog</a> von <a href="Aktin" title="Aktin">Aktin</a> und ein <a href="Scaffold-Proteine" class="mw-redirect" title="Scaffold-Proteine">Scaffold-Protein</a>,<sup id="cite_ref-pmid11032797”_2-0" class="reference"><a href="#cite_note-pmid11032797”-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> wie auch die Proteine <i>MreB</i>, <i>ParM</i> und <i>MamK</i>. Wie Aktin hydrolysiert FtsA <a href="Adenosintriphosphat" title="Adenosintriphosphat">Adenosintriphosphat</a> zur Änderung seiner <a href="Konformation" title="Konformation">Konformation</a> und bildet dann strangförmige Aggregate (<a href="Mikrofilament" class="mw-redirect" title="Mikrofilament">Mikrofilamente</a>) aus.<sup id="cite_ref-pmid22473211”_3-0" class="reference"><a href="#cite_note-pmid22473211”-3"><span class="cite-bracket">[</span>3<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid22111832_4-0" class="reference"><a href="#cite_note-pmid22111832-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup>
</p><p>FtsA ist strukturell ähnlich wie <i>PilM</i> aufgebaut, welches als <a href="ATPase" class="mw-redirect" title="ATPase">ATPase</a> des Typs IV in <a href="Pilus" title="Pilus">Pili</a> von Bakterien vorkommt.<sup id="cite_ref-pmid21596754”_5-0" class="reference"><a href="#cite_note-pmid21596754”-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup> FtsA bindet an <a href="FtsZ" class="mw-redirect" title="FtsZ">FtsZ</a> im <i>Z-Ring</i><sup id="cite_ref-pmid22473211”_3-1" class="reference"><a href="#cite_note-pmid22473211”-3"><span class="cite-bracket">[</span>3<span class="cite-bracket">]</span></a></sup> und bindet diesen über eine <a href="Amphiphilie" title="Amphiphilie">amphiphile</a> <a href="%CE%91-Helix" title="Α-Helix">α-Helix</a> am <a href="C-Terminus" title="C-Terminus"><i>C</i>-Terminus</a> des FtsA an die <a href="Zellmembran" title="Zellmembran">Zellmembran</a>.<sup id="cite_ref-pmid15752196”_6-0" class="reference"><a href="#cite_note-pmid15752196”-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid22111832_4-1" class="reference"><a href="#cite_note-pmid22111832-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> Alternativ kann der <i>C</i>-Terminus auch von <i>MinC</i> und <i>ZipA</i> gebunden werden. An einer anderen Stelle der Proteinoberfläche wird FtsN gebunden.<sup id="cite_ref-pmid15387815”_7-0" class="reference"><a href="#cite_note-pmid15387815”-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid22328664”_8-0" class="reference"><a href="#cite_note-pmid22328664”-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> FtsZ, FtsA und ZipA sind an der Einleitung der Zellbewegung beteiligt.<sup id="cite_ref-pmid23740256”_9-0" class="reference"><a href="#cite_note-pmid23740256”-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup> Während FtsA in <i><a href="Escherichia_coli" title="Escherichia coli">Escherichia coli</a></i> essentiell ist, kann seine Funktion in <i><a href="Bacillus_subtilis" title="Bacillus subtilis">Bacillus subtilis</a></i> bei einer <a href="Deletion" title="Deletion">Deletion</a> durch <i>SepF</i> teilweise kompensiert werden.<sup id="cite_ref-pmid16796675”_10-0" class="reference"><a href="#cite_note-pmid16796675”-10"><span class="cite-bracket">[</span>10<span class="cite-bracket">]</span></a></sup> Die <a href="Mutante" class="mw-redirect" title="Mutante">Mutante</a> <i>FtsA*</i> funktioniert unabhängig von <i>ZipA</i>.<sup id="cite_ref-pmid12634424”_11-0" class="reference"><a href="#cite_note-pmid12634424”-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid25213228”_12-0" class="reference"><a href="#cite_note-pmid25213228”-12"><span class="cite-bracket">[</span>12<span class="cite-bracket">]</span></a></sup> Andere identifizierte Mutanten besitzen veränderte <a href="Multimer" title="Multimer">Multimerisierungseigenschaften</a>.<sup id="cite_ref-pmid22111832_4-2" class="reference"><a href="#cite_note-pmid22111832-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> Die Funktionen des FtsA sind über verschiedene Bakterienarten <a href="Konservierung" title="Konservierung">konserviert</a>.<sup id="cite_ref-pmid24746687”_13-0" class="reference"><a href="#cite_note-pmid24746687”-13"><span class="cite-bracket">[</span>13<span class="cite-bracket">]</span></a></sup>
</p>
<div class="mw-heading mw-heading2"><h2 id="Einzelnachweise">Einzelnachweise</h2></div>
<ol class="references">
<li id="cite_note-pmid17322202”-1"><span class="mw-cite-backlink"><a href="#cite_ref-pmid17322202”_1-0">↑</a></span> <span class="reference-text">Geissler B, Shiomi D, Margolin W: <cite style="font-style:italic">The ftsA* gain-of-function allele of <i>Escherichia coli</i> and its effects on the stability and dynamics of the Z ring</cite>. In: <cite style="font-style:italic">Microbiology</cite>. 153. Jahrgang, Pt 3, 2007, <span style="white-space:nowrap">S.<span style="display:inline-block;width:.2em"> </span>814–823</span>, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1099/mic.0.2006%2F001834-0">10.1099/mic.0.2006/001834-0</a></span>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/17322202?dopt=Abstract">PMID 17322202</a>.<span class="Z3988" title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rfr_id=info:sid/de.wikipedia.org:FtsA&rft.atitle=The+ftsA%2A+gain-of-function+allele+of+Escherichia+coli+and+its+effects+on+the+stability+and+dynamics+of+the+Z+ring&rft.au=Geissler+B%2C+Shiomi+D%2C+Margolin+W&rft.date=2007&rft.doi=10.1099%2Fmic.0.2006%2F001834-0&rft.genre=journal&rft.issue=Pt+3&rft.jtitle=Microbiology&rft.pages=814-823&rft.pmid=17322202&rft.volume=153.+Jahrgang" style="display:none"> </span></span>
</li>
<li id="cite_note-pmid11032797”-2"><span class="mw-cite-backlink"><a href="#cite_ref-pmid11032797”_2-0">↑</a></span> <span class="reference-text">van den Ent F, Löwe J: <cite style="font-style:italic">Crystal structure of the cell division protein FtsA from <i>Thermotoga maritima</i></cite>. In: <cite style="font-style:italic"><a href="EMBO_J" class="mw-redirect" title="EMBO J">EMBO J</a></cite>. 19. Jahrgang, <span style="white-space:nowrap">Nr.<span style="display:inline-block;width:.2em"> </span>20</span>, 2000, <span style="white-space:nowrap">S.<span style="display:inline-block;width:.2em"> </span>5300–5307</span>, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1093/emboj%2F19.20.5300">10.1093/emboj/19.20.5300</a></span>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/11032797?dopt=Abstract">PMID 11032797</a>.<span class="Z3988" title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rfr_id=info:sid/de.wikipedia.org:FtsA&rft.atitle=Crystal+structure+of+the+cell+division+protein+FtsA+from+Thermotoga+maritima&rft.au=van+den+Ent+F%2C+L%C3%B6we+J&rft.date=2000&rft.doi=10.1093%2Femboj%2F19.20.5300&rft.genre=journal&rft.issue=20&rft.jtitle=EMBO+J&rft.pages=5300-5307&rft.pmid=11032797&rft.volume=19.+Jahrgang" style="display:none"> </span></span>
</li>
<li id="cite_note-pmid22473211”-3"><span class="mw-cite-backlink">↑ <sup><a href="#cite_ref-pmid22473211”_3-0">a</a></sup> <sup><a href="#cite_ref-pmid22473211”_3-1">b</a></sup></span> <span class="reference-text">Szwedziak P, Wang Q, Freund SMV, Löwe J: <cite style="font-style:italic">FtsA forms actin-like protofilaments</cite>. In: <cite style="font-style:italic">EMBO J</cite>. 31. Jahrgang, <span style="white-space:nowrap">Nr.<span style="display:inline-block;width:.2em"> </span>10</span>, 2012, <span style="white-space:nowrap">S.<span style="display:inline-block;width:.2em"> </span>2249–2260</span>, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1038/emboj.2012.76">10.1038/emboj.2012.76</a></span>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/22473211?dopt=Abstract">PMID 22473211</a>.<span class="Z3988" title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rfr_id=info:sid/de.wikipedia.org:FtsA&rft.atitle=FtsA+forms+actin-like+protofilaments&rft.au=Szwedziak+P%2C+Wang+Q%2C+Freund+SMV%2C+...&rft.date=2012&rft.doi=10.1038%2Femboj.2012.76&rft.genre=journal&rft.issue=10&rft.jtitle=EMBO+J&rft.pages=2249-2260&rft.pmid=22473211&rft.volume=31.+Jahrgang" style="display:none"> </span></span>
</li>
<li id="cite_note-pmid22111832-4"><span class="mw-cite-backlink">↑ <sup><a href="#cite_ref-pmid22111832_4-0">a</a></sup> <sup><a href="#cite_ref-pmid22111832_4-1">b</a></sup> <sup><a href="#cite_ref-pmid22111832_4-2">c</a></sup></span> <span class="reference-text">Pichoff S, Shen B, Sullivan B, Lutkenhaus J: <cite style="font-style:italic">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</cite>. In: <cite style="font-style:italic">Mol Microbiol</cite>. 83. Jahrgang, <span style="white-space:nowrap">Nr.<span style="display:inline-block;width:.2em"> </span>6</span>, 2012, <span style="white-space:nowrap">S.<span style="display:inline-block;width:.2em"> </span>151–167</span>, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1111/j.1365-2958.2011.07923.x">10.1111/j.1365-2958.2011.07923.x</a></span>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/22111832?dopt=Abstract">PMID 22111832</a>.<span class="Z3988" title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rfr_id=info:sid/de.wikipedia.org:FtsA&rft.atitle=FtsA+mutants+impaired+for+self-interaction+bypass+ZipA+suggesting+a+model+in+which+FtsA%E2%80%99s+self-interaction+competes+with+its+ability+to+recruit+downstream+division+proteins&rft.au=Pichoff+S%2C+Shen+B%2C+Sullivan+B%2C+...&rft.date=2012&rft.doi=10.1111%2Fj.1365-2958.2011.07923.x&rft.genre=journal&rft.issue=6&rft.jtitle=Mol+Microbiol&rft.pages=151-167&rft.pmid=22111832&rft.volume=83.+Jahrgang" style="display:none"> </span></span>
</li>
<li id="cite_note-pmid21596754”-5"><span class="mw-cite-backlink"><a href="#cite_ref-pmid21596754”_5-0">↑</a></span> <span class="reference-text">Karrupiah F, Derrick JP: <cite style="font-style:italic">Structure of the PilM-PilN inner membrane type IV pilus biogenesis complex from <i>Thermus thermophilus</i></cite>. In: <cite style="font-style:italic"><a href="J_Biol_Chem" class="mw-redirect" title="J Biol Chem">J Biol Chem</a></cite>. 286. Jahrgang, <span style="white-space:nowrap">Nr.<span style="display:inline-block;width:.2em"> </span>27</span>, 2011, <span style="white-space:nowrap">S.<span style="display:inline-block;width:.2em"> </span>24434–24442</span>, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1074/jbc.M111.243535">10.1074/jbc.M111.243535</a></span>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/21596754?dopt=Abstract">PMID 21596754</a>.<span class="Z3988" title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rfr_id=info:sid/de.wikipedia.org:FtsA&rft.atitle=Structure+of+the+PilM-PilN+inner+membrane+type+IV+pilus+biogenesis+complex+from+Thermus+thermophilus&rft.au=Karrupiah+F%2C+Derrick+JP&rft.date=2011&rft.doi=10.1074%2Fjbc.M111.243535&rft.genre=journal&rft.issue=27&rft.jtitle=J+Biol+Chem&rft.pages=24434-24442&rft.pmid=21596754&rft.volume=286.+Jahrgang" style="display:none"> </span></span>
</li>
<li id="cite_note-pmid15752196”-6"><span class="mw-cite-backlink"><a href="#cite_ref-pmid15752196”_6-0">↑</a></span> <span class="reference-text">Pichoff S, Lutkenhaus J: <cite style="font-style:italic">Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA</cite>. In: <cite style="font-style:italic">Mol Microbiol</cite>. 55. Jahrgang, <span style="white-space:nowrap">Nr.<span style="display:inline-block;width:.2em"> </span>6</span>, 2005, <span style="white-space:nowrap">S.<span style="display:inline-block;width:.2em"> </span>1722–1734</span>, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1111/j.1365-2958.2005.04522.x">10.1111/j.1365-2958.2005.04522.x</a></span>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/15752196?dopt=Abstract">PMID 15752196</a>.<span class="Z3988" title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rfr_id=info:sid/de.wikipedia.org:FtsA&rft.atitle=Tethering+the+Z+ring+to+the+membrane+through+a+conserved+membrane+targeting+sequence+in+FtsA&rft.au=Pichoff+S%2C+Lutkenhaus+J&rft.date=2005&rft.doi=10.1111%2Fj.1365-2958.2005.04522.x&rft.genre=journal&rft.issue=6&rft.jtitle=Mol+Microbiol&rft.pages=1722-1734&rft.pmid=15752196&rft.volume=55.+Jahrgang" style="display:none"> </span></span>
</li>
<li id="cite_note-pmid15387815”-7"><span class="mw-cite-backlink"><a href="#cite_ref-pmid15387815”_7-0">↑</a></span> <span class="reference-text">Rico AI, García-Ovalle M, Mingorance J, Vicente M: <cite style="font-style:italic">Role of two essential domains of Escherichia coli FtsA in localization and progression of the division ring</cite>. In: <cite style="font-style:italic">Mol Microbiol</cite>. 53. Jahrgang, <span style="white-space:nowrap">Nr.<span style="display:inline-block;width:.2em"> </span>5</span>, 1. September 2004, <span style="white-space:nowrap">S.<span style="display:inline-block;width:.2em"> </span>1359–1371year= 2004</span>, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1111/j.1365-2958.2004.04245.x">10.1111/j.1365-2958.2004.04245.x</a></span>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/15387815?dopt=Abstract">PMID 15387815</a>.<span class="Z3988" title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rfr_id=info:sid/de.wikipedia.org:FtsA&rft.atitle=Role+of+two+essential+domains+of+Escherichia+coli+FtsA+in+localization+and+progression+of+the+division+ring&rft.au=Rico+AI%2C+Garc%C3%ADa-Ovalle+M%2C+Mingorance+J%2C+...&rft.date=2004-09-01&rft.doi=10.1111%2Fj.1365-2958.2004.04245.x&rft.genre=journal&rft.issue=5&rft.jtitle=Mol+Microbiol&rft.pages=1359-1371year%3D+2004&rft.pmid=15387815&rft.volume=53.+Jahrgang" style="display:none"> </span></span>
</li>
<li id="cite_note-pmid22328664”-8"><span class="mw-cite-backlink"><a href="#cite_ref-pmid22328664”_8-0">↑</a></span> <span class="reference-text">Busiek KK, Eraso JM, Wang Y, Margolin W: <cite style="font-style:italic">The early divisome protein FtsA interacts directly through its 1c subdomain with the cytoplasmic domain of the late divisome protein FtsN</cite>. In: <cite style="font-style:italic">J Bacteriol</cite>. 194. Jahrgang, <span style="white-space:nowrap">Nr.<span style="display:inline-block;width:.2em"> </span>8</span>, 2012, <span style="white-space:nowrap">S.<span style="display:inline-block;width:.2em"> </span>1989–2000</span>, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1128/JB.06683-11">10.1128/JB.06683-11</a></span>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/22328664?dopt=Abstract">PMID 22328664</a>.<span class="Z3988" title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rfr_id=info:sid/de.wikipedia.org:FtsA&rft.atitle=The+early+divisome+protein+FtsA+interacts+directly+through+its+1c+subdomain+with+the+cytoplasmic+domain+of+the+late+divisome+protein+FtsN&rft.au=Busiek+KK%2C+Eraso+JM%2C+Wang+Y%2C+...&rft.date=2012&rft.doi=10.1128%2FJB.06683-11&rft.genre=journal&rft.issue=8&rft.jtitle=J+Bacteriol&rft.pages=1989-2000&rft.pmid=22328664&rft.volume=194.+Jahrgang" style="display:none"> </span></span>
</li>
<li id="cite_note-pmid23740256”-9"><span class="mw-cite-backlink"><a href="#cite_ref-pmid23740256”_9-0">↑</a></span> <span class="reference-text">Rico AI, Krupka M, Vicente M: <cite style="font-style:italic">In the beginning, <i>Escherichia coli</i> assembled the proto-ring: an initial phase of division</cite>. In: <cite style="font-style:italic">J Biol Chem</cite>. 288. Jahrgang, <span style="white-space:nowrap">Nr.<span style="display:inline-block;width:.2em"> </span>29</span>, 2013, <span style="white-space:nowrap">S.<span style="display:inline-block;width:.2em"> </span>20830–20836</span>, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1074/jbc.R113.479519">10.1074/jbc.R113.479519</a></span>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/23740256?dopt=Abstract">PMID 23740256</a>.<span class="Z3988" title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rfr_id=info:sid/de.wikipedia.org:FtsA&rft.atitle=In+the+beginning%2C+Escherichia+coli+assembled+the+proto-ring%3A+an+initial+phase+of+division&rft.au=Rico+AI%2C+Krupka+M%2C+Vicente+M&rft.date=2013&rft.doi=10.1074%2Fjbc.R113.479519&rft.genre=journal&rft.issue=29&rft.jtitle=J+Biol+Chem&rft.pages=20830-20836&rft.pmid=23740256&rft.volume=288.+Jahrgang" style="display:none"> </span></span>
</li>
<li id="cite_note-pmid16796675”-10"><span class="mw-cite-backlink"><a href="#cite_ref-pmid16796675”_10-0">↑</a></span> <span class="reference-text">Ishikawa S, Kawai Y, Hiramatsu K, Kuwano M, Ogasawara N: <cite style="font-style:italic">A new FtsZ-interacting protein, YlmF, complements the activity of FtsA during progression of cell division in <i>Bacillus subtilis</i></cite>. In: <cite style="font-style:italic">Mol Microbiol</cite>. 60. Jahrgang, <span style="white-space:nowrap">Nr.<span style="display:inline-block;width:.2em"> </span>1</span>, 2006, <span style="white-space:nowrap">S.<span style="display:inline-block;width:.2em"> </span>1364–1380</span>, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1111/j.1365-2958.2006.05184.x">10.1111/j.1365-2958.2006.05184.x</a></span>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/16796675?dopt=Abstract">PMID 16796675</a>.<span class="Z3988" title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rfr_id=info:sid/de.wikipedia.org:FtsA&rft.atitle=A+new+FtsZ-interacting+protein%2C+YlmF%2C+complements+the+activity+of+FtsA+during+progression+of+cell+division+in+Bacillus+subtilis&rft.au=Ishikawa+S%2C+Kawai+Y%2C+Hiramatsu+K%2C+...&rft.date=2006&rft.doi=10.1111%2Fj.1365-2958.2006.05184.x&rft.genre=journal&rft.issue=1&rft.jtitle=Mol+Microbiol&rft.pages=1364-1380&rft.pmid=16796675&rft.volume=60.+Jahrgang" style="display:none"> </span></span>
</li>
<li id="cite_note-pmid12634424”-11"><span class="mw-cite-backlink"><a href="#cite_ref-pmid12634424”_11-0">↑</a></span> <span class="reference-text">Geissler B, Elraheb D, Margolin W: <cite style="font-style:italic">A gain-of-function mutation in ftsA bypasses the requirement for the essential cell division gene zipA in <i>Escherichia coli</i></cite>. In: <cite style="font-style:italic"><a href="Proc_Natl_Acad_Sci_USA" class="mw-redirect" title="Proc Natl Acad Sci USA">Proc Natl Acad Sci USA</a></cite>. 100. Jahrgang, <span style="white-space:nowrap">Nr.<span style="display:inline-block;width:.2em"> </span>7</span>, 2003, <span style="white-space:nowrap">S.<span style="display:inline-block;width:.2em"> </span>4197–4202</span>, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1073/pnas.0635003100">10.1073/pnas.0635003100</a></span>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/12634424?dopt=Abstract">PMID 12634424</a>.<span class="Z3988" title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rfr_id=info:sid/de.wikipedia.org:FtsA&rft.atitle=A+gain-of-function+mutation+in+ftsA+bypasses+the+requirement+for+the+essential+cell+division+gene+zipA+in+Escherichia+coli&rft.au=Geissler+B%2C+Elraheb+D%2C+Margolin+W&rft.date=2003&rft.doi=10.1073%2Fpnas.0635003100&rft.genre=journal&rft.issue=7&rft.jtitle=Proc+Natl+Acad+Sci+USA&rft.pages=4197-4202&rft.pmid=12634424&rft.volume=100.+Jahrgang" style="display:none"> </span></span>
</li>
<li id="cite_note-pmid25213228”-12"><span class="mw-cite-backlink"><a href="#cite_ref-pmid25213228”_12-0">↑</a></span> <span class="reference-text">Osawa M, Erickson HP: <cite style="font-style:italic">Liposome division by a simple bacterial division machinery</cite>. In: <cite style="font-style:italic">Proc Natl Acad Sci USA</cite>. 110. Jahrgang, <span style="white-space:nowrap">Nr.<span style="display:inline-block;width:.2em"> </span>3</span>, 2013, <span style="white-space:nowrap">S.<span style="display:inline-block;width:.2em"> </span>11000–11004</span>, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1073/pnas.1222254110">10.1073/pnas.1222254110</a></span>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/25213228?dopt=Abstract">PMID 25213228</a>.<span class="Z3988" title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rfr_id=info:sid/de.wikipedia.org:FtsA&rft.atitle=Liposome+division+by+a+simple+bacterial+division+machinery&rft.au=Osawa+M%2C+Erickson+HP&rft.date=2013&rft.doi=10.1073%2Fpnas.1222254110&rft.genre=journal&rft.issue=3&rft.jtitle=Proc+Natl+Acad+Sci+USA&rft.pages=11000-11004&rft.pmid=25213228&rft.volume=110.+Jahrgang" style="display:none"> </span></span>
</li>
<li id="cite_note-pmid24746687”-13"><span class="mw-cite-backlink"><a href="#cite_ref-pmid24746687”_13-0">↑</a></span> <span class="reference-text">Fujita J, Maeda Y, Nagao C, Tsuchiya Y, Miyazaki Y, Hirose M, Mizohata E, Matsumoto Y, Inoue T, Mizuguchi K, Matsumura H: <cite style="font-style:italic">Crystal structure of FtsA from <i>Staphylococcus aureus</i></cite>. In: <cite style="font-style:italic"><a href="FEBS_Lett" class="mw-redirect" title="FEBS Lett">FEBS Lett</a></cite>. 588. Jahrgang, <span style="white-space:nowrap">Nr.<span style="display:inline-block;width:.2em"> </span>10</span>, 2014, <span style="white-space:nowrap">S.<span style="display:inline-block;width:.2em"> </span>1879–1885</span>, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1016/j.febslet.2014.04.008">10.1016/j.febslet.2014.04.008</a></span>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/24746687?dopt=Abstract">PMID 24746687</a>.<span class="Z3988" title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rfr_id=info:sid/de.wikipedia.org:FtsA&rft.atitle=Crystal+structure+of+FtsA+from+Staphylococcus+aureus&rft.au=Fujita+J%2C+Maeda+Y%2C+Nagao+C%2C+...&rft.date=2014&rft.doi=10.1016%2Fj.febslet.2014.04.008&rft.genre=journal&rft.issue=10&rft.jtitle=FEBS+Lett&rft.pages=1879-1885&rft.pmid=24746687&rft.volume=588.+Jahrgang" style="display:none"> </span></span>
</li>
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