Escherichia coli K-12 substr. MG1655 Polypeptide: essential cell division protein FtsK

Gene: ftsK Accession Numbers: G6464 (EcoCyc), b0890, ECK0881

Synonyms: dinH

Regulation Summary Diagram: ?

Regulation summary diagram for ftsK

FtsK is an essential cell division protein linking cell division and chromosome segregation [Kennedy08]. FtsK segregates the terminus region of sister chromosomes [Stouf13]. It acts as a DNA translocase at the division site and is required for unlinking chromosome dimers.

FtsK colocalizes with FtsZ to the septal ring structure; localization is dependent on FtsZ, FtsA and ZipA, but not FtsI and FtsQ [Yu98, Wang98d, Pichoff02]. Conversely, FtsQ, FtsL and FtsI require FtsK for localization to the Z ring [Chen01b]. The FtsK protein domains involved in the interactions with other cell division proteins have been mapped [Grenga08]. When FtsK is overexpressed, Z ring formation and cell division are inhibited [Draper98].

Although the hierarchy of dependency in the assembly of cell division proteins is largely linear, recent results showed that assembly of the cell division machinery is complex [Goehring05, Goehring06]. The requirement for FtsK for localization of FtsI is indirect [Geissler05]. Overexpression of FtsN partially restores localization of FtsL and FtsQ in the absence of FtsK [Goehring07a].

The FtsK protein is very large, and its membrane and cytoplasmic domains appear to have separable functions during cell division [Bigot04]. The N-terminal domain of FtsK, spanning ~200 amino acids, is sufficient for targeting FtsK to the septum [Yu98] and for its function in cell division [Draper98, Wang98d]. This domain shares some functional overlap with FtsQ, FtsB, FtsA, ZipA and FtsN and may be involved in the stability of the division protein machinery [Geissler05]. It contains four transmembrane helices linking two periplasmic loops, one of which contains a zinc metalloprotease consensus sequence that may [Dorazi00] or may not [Berezuk14] be required for function of FtsK. Refinement of FtsK membrane topology has revealed the presence of a periplasmic loop between TM3 and TM4 that is required for FtsK function [Berezuk14]. The N-terminal domain is sufficient for hexamerization of FtsN at midcell [Bisicchia13]. As long as it is targeted to the cell division septum, a truncated form of FtsK that lacks all transmembrane segments still functions in the resolution of chromosome dimers, indicating that DNA does not need to be transported through a pore formed by the transmembrane helices [Dubarry10].

Following the N-terminal membrane domain is a ~500 residue cytoplasmic linker region which may function in stabilizing the interactions of FtsK with other cell division proteins [Bigot04]. Two regions within this domain, 179-331 and 332-641, independently interact with FtsZ, FtsQ, FtsL and FtsI and were found to be required for normal septation [Dubarry10a].

The C-terminal domain of ~500 amino acids is cytoplasmic and involved in septation and chromosome partitioning [Liu98c, Yu98a, Steiner99a]. It can be separated into three domains, α, β and γ [Massey06]. The αβ domain contains a nucleotide binding motif belonging to the AAA family of ATPases [Begg95] and has ATP-dependent DNA translocase activity [Aussel02, Saleh04], which has been observed in single molecule assays [Pease05, Saleh05]. The translocation step size is ~2 bp per ATP [Graham10]. The chromosomal domain within which FtsK acts has been identified [Corre05, Deghorain11]. DNA translocation by FtsK is directional and is guided by octameric sequences (known as KOPS - FtsK Orienting Polar Sequences - in E. coli) [Bigot05, Levy05, Bigot06]. The γ domain is a DNA-binding winged-helix domain that recognizes KOPS [Sivanathan06]. KOPS appear to act only as FtsK loading sites and are not read during DNA translocation [Graham10]. Real-time imaging of FtsK activity showed that KOPS binding does not involve scanning along the DNA, and is enhanced in the presence of ADP and inhibited by ATP [Lee12c]. Failure to recognize KOPS has little effect in wild type E. coli, but more serious consequences in cell populations where chromosome dimers occur more frequently [Sivanathan09].

Although FtsK can displace proteins from DNA, DNA translocation by FtsK stops at XerCD-dif sites [Graham10a]. FtsK's DNA translocation activity and its ability to displace roadblocks on DNA can be separated [Crozat10]. Single-molecule real time imaging showed that, depending on their relative binding affinity, FtsK can push, displace, or bypass many other DNA-bound proteins. In contrast, an orientation-specific interaction between FtsK and XerD causes reversal of FtsK and prevents XerCD removal. Collision with RecBCD leads to reversal or displacement of FtsK, indicating that RecBCD is a more powerful motor protein than FtsK [Lee14b].

Recombination between sister chromosomes causes formation of chromosome dimers, which must be resolved by XerCD-mediated recombination between dif sites. The C-terminal domain of FtsK is required for this activity, activating the recombinase and actively positioning the dif sites [Aussel02, Capiaux02, Massey04, Yates06]. In particular, the γ regulatory subdomain activates the formation of a Holliday junction intermediate by XerD; it is proposed that this activation of unlinking is normally coupled to the translocation function of FtsK [Grainge11]. Single-molecule techniques have allowed observation of the activation of XerCD-dif recombination by FtsK [Zawadzki13, Diagne14]. A topological mechanism for the unlinking reaction has been proposed [Shimokawa13].

Newly replicated chromosomes are topologically linked and must be decatenated by Topo IV before they can be physically separated. FtsK and Topo IV interact physically via the ParC subunit of Topo IV. Functionally, the C-terminal domain of FtsK stimulates the decatenation activity of Topo IV on positively supercoiled DNA [Espeli03, Bigot10], but not the activity of DNA gyrase [Espeli03]. Unlinking of chromosomes can also be accomplished by step-wise XerCD-dif recombination in the presence of chromosomal translocation by FtsK [Grainge07]. Unexpectedly, FtsK antagonizes Ter-induced recombination [Louarn07].

The crystal structure of a monomeric point mutant of the motor domain has been solved at 2.7 Å resolution [Massey06], and a solution structure of the γ winged-helix domain was obtained [Sivanathan06].

The cell division defect of an ftsK ts mutant, but not a deletion mutant, can be suppressed specifically by deletion of dacA, which encodes PBP5 (peptidoglycan-modifying D-alanine:D-alanine carboxypeptidase) [Begg95, Draper98]. A deletion of ftsK can be partially suppressed by overproduction of FtsN [Draper98].

ftsK expression is increased as part of the SOS response, conferring increased resistance to DNA damage [Wang98d].

Selected reviews: [Grainge13, ReyesLamothe12, Kaimer11, Crozat10a, Sherratt10, Allemand09, Bigot07, Strick06, Lesterlin04, Weiss04, Sherratt04, Errington03, Donachie02]

Citations: [Lesterlin08]

Locations: inner membrane

Map Position: [932,447 -> 936,436] (20.1 centisomes, 72°)
Length: 3990 bp / 1329 aa

Molecular Weight of Polypeptide: 146.66 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0003027 , DIP:DIP-9703N , EchoBASE:EB3016 , EcoGene:EG13226 , EcoliWiki:b0890 , Mint:MINT-1261773 , ModBase:P46889 , OU-Microarray:b0890 , PortEco:ftsK , PR:PRO_000022719 , Pride:P46889 , Protein Model Portal:P46889 , RefSeq:NP_415410 , RegulonDB:G6464 , SMR:P46889 , String:511145.b0890 , UniProt:P46889

Relationship Links: InterPro:IN-FAMILY:IPR002543 , InterPro:IN-FAMILY:IPR018541 , InterPro:IN-FAMILY:IPR025199 , InterPro:IN-FAMILY:IPR027417 , PDB:Structure:2IUS , PDB:Structure:2J5P , Pfam:IN-FAMILY:PF01580 , Pfam:IN-FAMILY:PF09397 , Pfam:IN-FAMILY:PF13491 , Prosite:IN-FAMILY:PS50901 , Smart:IN-FAMILY:SM00843

Genetic Regulation Schematic: ?

Genetic regulation schematic for ftsK

GO Terms:

Biological Process: GO:0000920 - cell separation after cytokinesis Inferred from experiment [Diez97]
GO:0006970 - response to osmotic stress Inferred from experiment [Diez97]
GO:0007059 - chromosome segregation Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01, Graham10a, Grainge07, Capiaux02, Yu98a]
GO:0008152 - metabolic process Inferred from experiment [Bigot10, Graham10a, Bonne09, Lowe08, Massey06, Levy05]
GO:0009651 - response to salt stress Inferred from experiment [Diez97]
GO:0043085 - positive regulation of catalytic activity Inferred from experiment [Grainge11]
GO:0045893 - positive regulation of transcription, DNA-templated Inferred from experiment [Diez97]
GO:0051301 - cell division Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01, Dubarry10a, Yu98a, Draper98, Diez97, Begg95]
GO:0071236 - cellular response to antibiotic Inferred from experiment [Wang98d]
GO:0007049 - cell cycle Inferred by computational analysis [UniProtGOA11, GOA01]
Molecular Function: GO:0003677 - DNA binding Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01, Lowe08]
GO:0005515 - protein binding Inferred from experiment [DUlisse07, Grenga08]
GO:0015616 - DNA translocase activity Inferred from experiment [Graham10a, Bonne09, Levy05]
GO:0016887 - ATPase activity Inferred from experiment [Bigot10, Graham10a, Lowe08]
GO:0033676 - double-stranded DNA-dependent ATPase activity Inferred from experiment [Massey06]
GO:0042802 - identical protein binding Inferred from experiment [Bisicchia13]
GO:0043565 - sequence-specific DNA binding Inferred from experiment [Sivanathan06, Ptacin06]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11, GOA01]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, DiazMejia09, Daley05, Dorazi00]
GO:0005887 - integral component of plasma membrane Inferred from experiment [Dorazi00]
GO:0016020 - membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, Wang98d, Dorazi00]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11, GOA01]

MultiFun Terms: cell processes cell division
cell processes SOS response
cell structure membrane
transport Transporters of Unknown Classification

Essentiality data for ftsK knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 2]

Last-Curated ? 04-Aug-2014 by Keseler I , SRI International

Sequence Features

Protein sequence of essential cell division protein FtsK with features indicated

Feature Class Location Citations Comment
Transmembrane-Region 25 -> 44
[Berezuk14, UniProt14]
UniProt: Helical.
Mutagenesis-Variant 58
[Dorazi00, UniProt11]
UniProt: Loss of function.
Transmembrane-Region 75 -> 98
[Berezuk14, UniProt14]
UniProt: Helical.
Mutagenesis-Variant 80
UniProt: In Toe44; loss of function under extreme conditions.
Transmembrane-Region 116 -> 132
[Berezuk14, UniProt14]
UniProt: Helical.
Mutagenesis-Variant 135
[Berezuk14, UniProt14]
UniProt: Impairs the ability of FtsK to function in cell division. Uncouples invagination of the inner and outer membranes and results in cellular voids.
Mutagenesis-Variant 136
[Berezuk14, UniProt14]
UniProt: Impairs the ability of FtsK to function in cell division. Uncouples invagination of the inner and outer membranes and results in cellular voids.
Mutagenesis-Variant 137
[Berezuk14, UniProt14]
UniProt: Impairs the ability of FtsK to function in cell division. Uncouples invagination of the inner and outer membranes and results in cellular voids.
Mutagenesis-Variant 138
[Berezuk14, UniProt14]
UniProt: Impairs the ability of FtsK to function in cell division. Uncouples invagination of the inner and outer membranes and results in cellular voids.
Transmembrane-Region 163 -> 179
[Berezuk14, UniProt14]
UniProt: Helical.
Protein-Segment 184 -> 817
UniProt: Linker; Sequence Annotation Type: region of interest.
Protein-Segment 331 -> 822
UniProt: Gln/Glu/Pro-rich; Sequence Annotation Type: compositionally biased region;
Sequence-Conflict 333 -> 334
[Begg95, UniProt10a]
UniProt: (in Ref. 1; CAA90178);
Sequence-Conflict 388 -> 389
[Begg95, UniProt10a]
UniProt: (in Ref. 1; CAA90178);
Protein-Segment 818 -> 943
UniProt: Alpha; Sequence Annotation Type: region of interest.
Protein-Segment 944 -> 1258
UniProt: Beta; Sequence Annotation Type: region of interest.
Conserved-Region 974 -> 1187
UniProt: FtsK;
Nucleotide-Phosphate-Binding-Region 994 -> 999
UniProt: ATP; Non-Experimental Qualifier: by similarity.
Mutagenesis-Variant 997
[Bigot04, UniProt12]
UniProt: Does not activate Xer recombination.
Sequence-Conflict 1101 -> 1103
[Begg95, UniProt10a]
UniProt: (in Ref. 1; CAA90178);
Sequence-Conflict 1193
[Begg95, UniProt10a]
UniProt: (in Ref. 1; CAA90178);
Protein-Segment 1259 -> 1329
UniProt: Gamma; Sequence Annotation Type: region of interest.

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Units:

Transcription-unit diagram

Transcription-unit diagram


Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


Allemand09: Allemand JF, Maier B (2009). "Bacterial translocation motors investigated by single molecule techniques." FEMS Microbiol Rev 33(3);593-610. PMID: 19243443

Aussel02: Aussel L, Barre FX, Aroyo M, Stasiak A, Stasiak AZ, Sherratt D (2002). "FtsK Is a DNA motor protein that activates chromosome dimer resolution by switching the catalytic state of the XerC and XerD recombinases." Cell 108(2);195-205. PMID: 11832210

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Begg95: Begg KJ, Dewar SJ, Donachie WD (1995). "A new Escherichia coli cell division gene, ftsK." J Bacteriol 177(21);6211-22. PMID: 7592387

Berezuk14: Berezuk AM, Goodyear M, Khursigara CM (2014). "Site-directed fluorescence labeling reveals a revised N-terminal membrane topology and functional periplasmic residues in the Escherichia coli cell division protein FtsK." J Biol Chem. PMID: 25002583

Bigot04: Bigot S, Corre J, Louarn JM, Cornet F, Barre FX (2004). "FtsK activities in Xer recombination, DNA mobilization and cell division involve overlapping and separate domains of the protein." Mol Microbiol 54(4);876-86. PMID: 15522074

Bigot05: Bigot S, Saleh OA, Lesterlin C, Pages C, El Karoui M, Dennis C, Grigoriev M, Allemand JF, Barre FX, Cornet F (2005). "KOPS: DNA motifs that control E. coli chromosome segregation by orienting the FtsK translocase." EMBO J 24(21);3770-80. PMID: 16211009

Bigot06: Bigot S, Saleh OA, Cornet F, Allemand JF, Barre FX (2006). "Oriented loading of FtsK on KOPS." Nat Struct Mol Biol 13(11);1026-8. PMID: 17041597

Bigot07: Bigot S, Sivanathan V, Possoz C, Barre FX, Cornet F (2007). "FtsK, a literate chromosome segregation machine." Mol Microbiol 64(6);1434-41. PMID: 17511809

Bigot10: Bigot S, Marians KJ (2010). "DNA chirality-dependent stimulation of topoisomerase IV activity by the C-terminal AAA+ domain of FtsK." Nucleic Acids Res 38(9);3031-40. PMID: 20081205

Bisicchia13: Bisicchia P, Steel B, Mariam Debela MH, Lowe J, Sherratt D (2013). "The N-terminal membrane-spanning domain of the Escherichia coli DNA translocase FtsK hexamerizes at midcell." MBio 4(6);e00800-13. PMID: 24302254

Bonne09: Bonne L, Bigot S, Chevalier F, Allemand JF, Barre FX (2009). "Asymmetric DNA requirements in Xer recombination activation by FtsK." Nucleic Acids Res 37(7);2371-80. PMID: 19246541

Capiaux02: Capiaux H, Lesterlin C, Perals K, Louarn JM, Cornet F (2002). "A dual role for the FtsK protein in Escherichia coli chromosome segregation." EMBO Rep 3(6);532-6. PMID: 12034757

Chen01b: Chen JC, Beckwith J (2001). "FtsQ, FtsL and FtsI require FtsK, but not FtsN, for co-localization with FtsZ during Escherichia coli cell division." Mol Microbiol 42(2);395-413. PMID: 11703663

Corre05: Corre J, Louarn JM (2005). "Extent of the activity domain and possible roles of FtsK in the Escherichia coli chromosome terminus." Mol Microbiol 56(6);1539-48. PMID: 15916604

Crozat10: Crozat E, Meglio A, Allemand JF, Chivers CE, Howarth M, Venien-Bryan C, Grainge I, Sherratt DJ (2010). "Separating speed and ability to displace roadblocks during DNA translocation by FtsK." EMBO J 29(8);1423-33. PMID: 20379135

Crozat10a: Crozat E, Grainge I (2010). "FtsK DNA translocase: the fast motor that knows where it's going." Chembiochem 11(16);2232-43. PMID: 20922738

Daley05: Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308(5726);1321-3. PMID: 15919996

Deghorain11: Deghorain M, Pages C, Meile JC, Stouf M, Capiaux H, Mercier R, Lesterlin C, Hallet B, Cornet F (2011). "A defined terminal region of the E. coli chromosome shows late segregation and high FtsK activity." PLoS One 6(7);e22164. PMID: 21799784

Diagne14: Diagne CT, Salhi M, Crozat E, Salome L, Cornet F, Rousseau P, Tardin C (2014). "TPM analyses reveal that FtsK contributes both to the assembly and the activation of the XerCD-dif recombination synapse." Nucleic Acids Res 42(3);1721-32. PMID: 24214995

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Diez97: Diez AA, Farewell A, Nannmark U, Nystrom T (1997). "A mutation in the ftsK gene of Escherichia coli affects cell-cell separation, stationary-phase survival, stress adaptation, and expression of the gene encoding the stress protein UspA." J Bacteriol 179(18);5878-83. PMID: 9294448

Donachie02: Donachie WD (2002). "FtsK: Maxwell's Demon?." Mol Cell 9(2);206-7. PMID: 11864592

Dorazi00: Dorazi R, Dewar SJ (2000). "Membrane topology of the N-terminus of the Escherichia coli FtsK division protein." FEBS Lett 478(1-2);13-8. PMID: 10922461

Draper98: Draper GC, McLennan N, Begg K, Masters M, Donachie WD (1998). "Only the N-terminal domain of FtsK functions in cell division." J Bacteriol 180(17);4621-7. PMID: 9721304

Dubarry10: Dubarry N, Barre FX (2010). "Fully efficient chromosome dimer resolution in Escherichia coli cells lacking the integral membrane domain of FtsK." EMBO J 29(3);597-605. PMID: 20033058

Dubarry10a: Dubarry N, Possoz C, Barre FX (2010). "Multiple regions along the Escherichia coli FtsK protein are implicated in cell division." Mol Microbiol 78(5);1088-100. PMID: 21091498

DUlisse07: D'Ulisse V, Fagioli M, Ghelardini P, Paolozzi L (2007). "Three functional subdomains of the Escherichia coli FtsQ protein are involved in its interaction with the other division proteins." Microbiology 153(Pt 1);124-38. PMID: 17185541

Errington03: Errington J, Daniel RA, Scheffers DJ (2003). "Cytokinesis in bacteria." Microbiol Mol Biol Rev 67(1);52-65. PMID: 12626683

Espeli03: Espeli O, Lee C, Marians KJ (2003). "A physical and functional interaction between Escherichia coli FtsK and topoisomerase IV." J Biol Chem 278(45);44639-44. PMID: 12939258

Geissler05: Geissler B, Margolin W (2005). "Evidence for functional overlap among multiple bacterial cell division proteins: compensating for the loss of FtsK." Mol Microbiol 58(2);596-612. PMID: 16194242

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Goehring05: Goehring NW, Gueiros-Filho F, Beckwith J (2005). "Premature targeting of a cell division protein to midcell allows dissection of divisome assembly in Escherichia coli." Genes Dev 19(1);127-37. PMID: 15630023

Goehring06: Goehring NW, Gonzalez MD, Beckwith J (2006). "Premature targeting of cell division proteins to midcell reveals hierarchies of protein interactions involved in divisome assembly." Mol Microbiol 61(1);33-45. PMID: 16824093

Goehring07a: Goehring NW, Robichon C, Beckwith J (2007). "Role for the nonessential N terminus of FtsN in divisome assembly." J Bacteriol 189(2);646-9. PMID: 17071748

Graham10: Graham JE, Sherratt DJ, Szczelkun MD (2010). "Sequence-specific assembly of FtsK hexamers establishes directional translocation on DNA." Proc Natl Acad Sci U S A 107(47);20263-8. PMID: 21048089

Graham10a: Graham JE, Sivanathan V, Sherratt DJ, Arciszewska LK (2010). "FtsK translocation on DNA stops at XerCD-dif." Nucleic Acids Res 38(1);72-81. PMID: 19854947

Grainge07: Grainge I, Bregu M, Vazquez M, Sivanathan V, Ip SC, Sherratt DJ (2007). "Unlinking chromosome catenanes in vivo by site-specific recombination." EMBO J 26(19);4228-38. PMID: 17805344

Grainge11: Grainge I, Lesterlin C, Sherratt DJ (2011). "Activation of XerCD-dif recombination by the FtsK DNA translocase." Nucleic Acids Res 39(12);5140-8. PMID: 21371996

Grainge13: Grainge I (2013). "Simple topology: FtsK-directed recombination at the dif site." Biochem Soc Trans 41(2);595-600. PMID: 23514160

Grenga08: Grenga L, Luzi G, Paolozzi L, Ghelardini P (2008). "The Escherichia coli FtsK functional domains involved in its interaction with its divisome protein partners." FEMS Microbiol Lett 287(2);163-7. PMID: 18759781

Kaimer11: Kaimer C, Graumann PL (2011). "Players between the worlds: multifunctional DNA translocases." Curr Opin Microbiol 14(6);719-25. PMID: 22047950

Kennedy08: Kennedy SP, Chevalier F, Barre FX (2008). "Delayed activation of Xer recombination at dif by FtsK during septum assembly in Escherichia coli." Mol Microbiol 68(4);1018-28. PMID: 18363794

Lee12c: Lee JY, Finkelstein IJ, Crozat E, Sherratt DJ, Greene EC (2012). "Single-molecule imaging of DNA curtains reveals mechanisms of KOPS sequence targeting by the DNA translocase FtsK." Proc Natl Acad Sci U S A 109(17);6531-6. PMID: 22493241

Lee14b: Lee JY, Finkelstein IJ, Arciszewska LK, Sherratt DJ, Greene EC (2014). "Single-molecule imaging of FtsK translocation reveals mechanistic features of protein-protein collisions on DNA." Mol Cell 54(5);832-43. PMID: 24768536

Lesterlin04: Lesterlin C, Barre FX, Cornet F (2004). "Genetic recombination and the cell cycle: what we have learned from chromosome dimers." Mol Microbiol 54(5);1151-60. PMID: 15554958

Lesterlin08: Lesterlin C, Pages C, Dubarry N, Dasgupta S, Cornet F (2008). "Asymmetry of chromosome Replichores renders the DNA translocase activity of FtsK essential for cell division and cell shape maintenance in Escherichia coli." PLoS Genet 4(12);e1000288. PMID: 19057667

Levy05: Levy O, Ptacin JL, Pease PJ, Gore J, Eisen MB, Bustamante C, Cozzarelli NR (2005). "Identification of oligonucleotide sequences that direct the movement of the Escherichia coli FtsK translocase." Proc Natl Acad Sci U S A 102(49);17618-23. PMID: 16301526

Liu98c: Liu G, Draper GC, Donachie WD (1998). "FtsK is a bifunctional protein involved in cell division and chromosome localization in Escherichia coli." Mol Microbiol 29(3);893-903. PMID: 9723927

Louarn07: Louarn JM, Quentin Y (2007). "FtsK controls metastable recombination provoked by an extra Ter site in the Escherichia coli chromosome terminus." Mol Microbiol 64(1);207-19. PMID: 17376083

Lowe08: Lowe J, Ellonen A, Allen MD, Atkinson C, Sherratt DJ, Grainge I (2008). "Molecular mechanism of sequence-directed DNA loading and translocation by FtsK." Mol Cell 31(4);498-509. PMID: 18722176

Massey04: Massey TH, Aussel L, Barre FX, Sherratt DJ (2004). "Asymmetric activation of Xer site-specific recombination by FtsK." EMBO Rep 5(4);399-404. PMID: 15031713

Massey06: Massey TH, Mercogliano CP, Yates J, Sherratt DJ, Lowe J (2006). "Double-stranded DNA translocation: structure and mechanism of hexameric FtsK." Mol Cell 23(4);457-69. PMID: 16916635

Pease05: Pease PJ, Levy O, Cost GJ, Gore J, Ptacin JL, Sherratt D, Bustamante C, Cozzarelli NR (2005). "Sequence-directed DNA translocation by purified FtsK." Science 307(5709);586-90. PMID: 15681387

Pichoff02: Pichoff S, Lutkenhaus J (2002). "Unique and overlapping roles for ZipA and FtsA in septal ring assembly in Escherichia coli." EMBO J 21(4);685-93. PMID: 11847116

Ptacin06: Ptacin JL, Nollmann M, Bustamante C, Cozzarelli NR (2006). "Identification of the FtsK sequence-recognition domain." Nat Struct Mol Biol 13(11);1023-5. PMID: 17041598

ReyesLamothe12: Reyes-Lamothe R, Nicolas E, Sherratt DJ (2012). "Chromosome replication and segregation in bacteria." Annu Rev Genet 46;121-43. PMID: 22934648

Saleh04: Saleh OA, Perals C, Barre FX, Allemand JF (2004). "Fast, DNA-sequence independent translocation by FtsK in a single-molecule experiment." EMBO J 23(12);2430-9. PMID: 15167891

Saleh05: Saleh OA, Bigot S, Barre FX, Allemand JF (2005). "Analysis of DNA supercoil induction by FtsK indicates translocation without groove-tracking." Nat Struct Mol Biol 12(5);436-40. PMID: 15821742

Sherratt04: Sherratt DJ, Soballe B, Barre FX, Filipe S, Lau I, Massey T, Yates J (2004). "Recombination and chromosome segregation." Philos Trans R Soc Lond B Biol Sci 359(1441);61-9. PMID: 15065657

Sherratt10: Sherratt DJ, Arciszewska LK, Crozat E, Graham JE, Grainge I (2010). "The Escherichia coli DNA translocase FtsK." Biochem Soc Trans 38(2);395-8. PMID: 20298190

Shimokawa13: Shimokawa K, Ishihara K, Grainge I, Sherratt DJ, Vazquez M (2013). "FtsK-dependent XerCD-dif recombination unlinks replication catenanes in a stepwise manner." Proc Natl Acad Sci U S A 110(52);20906-11. PMID: 24218579

Sivanathan06: Sivanathan V, Allen MD, de Bekker C, Baker R, Arciszewska LK, Freund SM, Bycroft M, Lowe J, Sherratt DJ (2006). "The FtsK gamma domain directs oriented DNA translocation by interacting with KOPS." Nat Struct Mol Biol 13(11);965-72. PMID: 17057717

Sivanathan09: Sivanathan V, Emerson JE, Pages C, Cornet F, Sherratt DJ, Arciszewska LK (2009). "KOPS-guided DNA translocation by FtsK safeguards Escherichia coli chromosome segregation." Mol Microbiol 71(4);1031-42. PMID: 19170870

Steiner99a: Steiner W, Liu G, Donachie WD, Kuempel P (1999). "The cytoplasmic domain of FtsK protein is required for resolution of chromosome dimers." Mol Microbiol 31(2);579-83. PMID: 10027974

Stouf13: Stouf M, Meile JC, Cornet F (2013). "FtsK actively segregates sister chromosomes in Escherichia coli." Proc Natl Acad Sci U S A 110(27);11157-62. PMID: 23781109

Strick06: Strick TR, Quessada-Vial A (2006). "FtsK: a groovy helicase." Nat Struct Mol Biol 13(11);948-50. PMID: 17082786

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProt12: UniProt Consortium (2012). "UniProt version 2012-09 released on 2012-09-12 00:00:00." Database.

UniProt12b: UniProt Consortium (2012). "UniProt version 2012-02 released on 2012-02-29 00:00:00." Database.

UniProt14: UniProt Consortium (2014). "UniProt version 2014-08 released on 2014-08-01 00:00:00." Database.

UniProt15: UniProt Consortium (2015). "UniProt version 2015-01 released on 2015-01-16 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

Wang98d: Wang L, Lutkenhaus J (1998). "FtsK is an essential cell division protein that is localized to the septum and induced as part of the SOS response." Mol Microbiol 29(3);731-40. PMID: 9723913

Weiss04: Weiss DS (2004). "Bacterial cell division and the septal ring." Mol Microbiol 54(3);588-97. PMID: 15491352

Yates06: Yates J, Zhekov I, Baker R, Eklund B, Sherratt DJ, Arciszewska LK (2006). "Dissection of a functional interaction between the DNA translocase, FtsK, and the XerD recombinase." Mol Microbiol 59(6);1754-66. PMID: 16553881

Yu98: Yu XC, Tran AH, Sun Q, Margolin W (1998). "Localization of cell division protein FtsK to the Escherichia coli septum and identification of a potential N-terminal targeting domain." J Bacteriol 180(5);1296-304. PMID: 9495771

Yu98a: Yu XC, Weihe EK, Margolin W (1998). "Role of the C terminus of FtsK in Escherichia coli chromosome segregation." J Bacteriol 180(23);6424-8. PMID: 9829960

Zawadzki13: Zawadzki P, May PF, Baker RA, Pinkney JN, Kapanidis AN, Sherratt DJ, Arciszewska LK (2013). "Conformational transitions during FtsK translocase activation of individual XerCD-dif recombination complexes." Proc Natl Acad Sci U S A 110(43);17302-7. PMID: 24101525

Other References Related to Gene Regulation

Dorazi00a: Dorazi R, Dewar SJ (2000). "The SOS promoter dinH is essential for ftsK transcription during cell division." Microbiology 146 ( Pt 11);2891-9. PMID: 11065367

Lewis92: Lewis LK, Jenkins ME, Mount DW (1992). "Isolation of DNA damage-inducible promoters in Escherichia coli: regulation of polB (dinA), dinG, and dinH by LexA repressor." J Bacteriol 174(10);3377-85. PMID: 1577702

Lewis94: Lewis LK, Harlow GR, Gregg-Jolly LA, Mount DW (1994). "Identification of high affinity binding sites for LexA which define new DNA damage-inducible genes in Escherichia coli." J Mol Biol 241(4);507-23. PMID: 8057377

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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