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Protein

DNA translocase FtsK

Gene

ftsK

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the replication terminus region. Translocation stops specifically at Xer-dif sites, where FtsK interacts with the Xer recombinase, allowing activation of chromosome unlinking by recombination. FtsK orienting polar sequences (KOPS) guide the direction of DNA translocation. FtsK can remove proteins from DNA as it translocates, but translocation stops specifically at XerCD-dif site, thereby preventing removal of XerC and XerD from dif. Stoppage of translocation is accompanied by a reduction in ATPase activity. Also stimulates topoisomerase 4 activity. Required for the targeting of FtsQ, FtsL and FtsI to the septum.11 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi994 – 9996ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATPase activity Source: CACAO
  • ATP binding Source: UniProtKB-KW
  • DNA binding Source: EcoliWiki
  • DNA translocase activity Source: EcoCyc
  • double-stranded DNA-dependent ATPase activity Source: CACAO
  • identical protein binding Source: EcoCyc
  • sequence-specific DNA binding Source: EcoCyc

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cell division Source: CACAO
  • cell separation after cytokinesis Source: EcoliWiki
  • cellular response to antibiotic Source: EcoliWiki
  • chromosome segregation Source: EcoliWiki
  • positive regulation of catalytic activity Source: EcoCyc
  • positive regulation of transcription, DNA-templated Source: EcoliWiki
  • response to osmotic stress Source: EcoliWiki
  • response to salt stress Source: EcoliWiki
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Chromosome partition

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:G6464-MONOMER.
ECOL316407:JW0873-MONOMER.

Protein family/group databases

TCDBi3.A.12.1.2. the septal dna translocator (s-dna-t) family.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA translocase FtsK
Gene namesi
Name:ftsK
Ordered Locus Names:b0890, JW0873
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13226. ftsK.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2424Cytoplasmic1 PublicationAdd
BLAST
Transmembranei25 – 4420Helical1 PublicationAdd
BLAST
Topological domaini45 – 7430Periplasmic1 PublicationAdd
BLAST
Transmembranei75 – 9824Helical1 PublicationAdd
BLAST
Topological domaini99 – 11517Cytoplasmic1 PublicationAdd
BLAST
Transmembranei116 – 13217Helical1 PublicationAdd
BLAST
Topological domaini133 – 16230Periplasmic1 PublicationAdd
BLAST
Transmembranei163 – 17917Helical1 PublicationAdd
BLAST
Topological domaini180 – 13291150Cytoplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: EcoCyc
  • membrane Source: EcoliWiki
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi58 – 581E → A: Loss of function. 1 Publication
Mutagenesisi80 – 801G → A in Toe44; loss of function under extreme conditions.
Mutagenesisi135 – 1351D → C: Impairs the ability of FtsK to function in cell division. Uncouples invagination of the inner and outer membranes and results in cellular voids. 1 Publication
Mutagenesisi136 – 1361D → C: Impairs the ability of FtsK to function in cell division. Uncouples invagination of the inner and outer membranes and results in cellular voids. 1 Publication
Mutagenesisi137 – 1371I → C: Impairs the ability of FtsK to function in cell division. Uncouples invagination of the inner and outer membranes and results in cellular voids. 1 Publication
Mutagenesisi138 – 1381W → C: Impairs the ability of FtsK to function in cell division. Uncouples invagination of the inner and outer membranes and results in cellular voids. 1 Publication
Mutagenesisi997 – 9971K → A: Does not activate Xer recombination. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13291329DNA translocase FtsKPRO_0000098257Add
BLAST

Proteomic databases

PaxDbiP46889.
PRIDEiP46889.

Expressioni

Inductioni

Induced by DNA-damaging agents.1 Publication

Interactioni

Subunit structurei

Homohexamer. Forms a ring that surrounds DNA. Interacts with FtsZ, FtsQ, FtsL and FtsI.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ftsQP061363EBI-550795,EBI-1130157

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4260652. 426 interactions.
DIPiDIP-9703N.
IntActiP46889. 7 interactions.
MINTiMINT-1261773.
STRINGi511145.b0890.

Structurei

Secondary structure

1
1329
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi843 – 8453Combined sources
Helixi859 – 87214Combined sources
Turni873 – 8764Combined sources
Beta strandi879 – 8868Combined sources
Beta strandi888 – 89710Combined sources
Helixi904 – 9074Combined sources
Helixi910 – 9167Combined sources
Beta strandi923 – 9264Combined sources
Beta strandi931 – 9399Combined sources
Helixi948 – 9525Combined sources
Helixi955 – 9584Combined sources
Beta strandi965 – 9717Combined sources
Beta strandi976 – 9805Combined sources
Helixi981 – 9833Combined sources
Beta strandi986 – 9905Combined sources
Helixi997 – 100913Combined sources
Turni1014 – 10163Combined sources
Beta strandi1017 – 10226Combined sources
Beta strandi1025 – 10273Combined sources
Helixi1028 – 10325Combined sources
Beta strandi1038 – 10414Combined sources
Helixi1046 – 106924Combined sources
Helixi1075 – 108713Combined sources
Beta strandi1115 – 11217Combined sources
Helixi1123 – 114422Combined sources
Helixi1146 – 11483Combined sources
Beta strandi1150 – 11578Combined sources
Turni1161 – 11633Combined sources
Helixi1166 – 11716Combined sources
Beta strandi1174 – 11785Combined sources
Helixi1183 – 11908Combined sources
Beta strandi1191 – 11933Combined sources
Helixi1195 – 11973Combined sources
Beta strandi1203 – 12075Combined sources
Beta strandi1215 – 12195Combined sources
Helixi1224 – 123512Combined sources
Turni1262 – 12643Combined sources
Helixi1269 – 127810Combined sources
Beta strandi1281 – 12833Combined sources
Helixi1284 – 12918Combined sources
Helixi1295 – 130814Combined sources
Beta strandi1316 – 13227Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IUSX-ray2.70A/B/C/D/E/F818-1329[»]
2J5PNMR-A1261-1329[»]
ProteinModelPortaliP46889.
SMRiP46889. Positions 840-1248, 1261-1329.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46889.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini974 – 1187214FtsKPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni184 – 817634LinkerAdd
BLAST
Regioni818 – 943126AlphaAdd
BLAST
Regioni944 – 1258315BetaAdd
BLAST
Regioni1259 – 132971GammaAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi331 – 822492Gln/Glu/Pro-richAdd
BLAST

Domaini

Consists of an N-terminal domain, which is sufficient for the localization to the septal ring and is required for cell division, followed by a linker domain, and a C-terminal domain, which forms the translocation motor involved in chromosome segregation. The C-terminal domain can be further subdivided into alpha, beta and gamma subdomains. The alpha and beta subdomains multimerise to produce a hexameric ring, contain the nucleotide binding motif and form the DNA pump. The gamma subdomain is a regulatory subdomain that controls translocation of DNA by recognition of KOPS motifs and interacts with XerD recombinase.6 Publications

Sequence similaritiesi

Belongs to the FtsK/SpoIIIE/SftA family.Curated
Contains 1 FtsK domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105CNU. Bacteria.
COG1674. LUCA.
HOGENOMiHOG000010001.
InParanoidiP46889.
KOiK03466.
OMAiDPFWKPG.
OrthoDBiEOG6S52GD.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR025199. FtsK_4TM.
IPR002543. FtsK_dom.
IPR018541. Ftsk_gamma.
IPR027417. P-loop_NTPase.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF13491. FtsK_4TM. 1 hit.
PF09397. Ftsk_gamma. 1 hit.
PF01580. FtsK_SpoIIIE. 1 hit.
[Graphical view]
SMARTiSM00843. Ftsk_gamma. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50901. FTSK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P46889-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQEYIEDKE VTLTKLSSGR RLLEALLILI VLFAVWLMAA LLSFNPSDPS
60 70 80 90 100
WSQTAWHEPI HNLGGMPGAW LADTLFFIFG VMAYTIPVII VGGCWFAWRH
110 120 130 140 150
QSSDEYIDYF AVSLRIIGVL ALILTSCGLA AINADDIWYF ASGGVIGSLL
160 170 180 190 200
STTLQPLLHS SGGTIALLCV WAAGLTLFTG WSWVTIAEKL GGWILNILTF
210 220 230 240 250
ASNRTRRDDT WVDEDEYEDD EEYEDENHGK QHESRRARIL RGALARRKRL
260 270 280 290 300
AEKFINPMGR QTDAALFSGK RMDDDEEITY TARGVAADPD DVLFSGNRAT
310 320 330 340 350
QPEYDEYDPL LNGAPITEPV AVAAAATTAT QSWAAPVEPV TQTPPVASVD
360 370 380 390 400
VPPAQPTVAW QPVPGPQTGE PVIAPAPEGY PQQSQYAQPA VQYNEPLQQP
410 420 430 440 450
VQPQQPYYAP AAEQPAQQPY YAPAPEQPVA GNAWQAEEQQ STFAPQSTYQ
460 470 480 490 500
TEQTYQQPAA QEPLYQQPQP VEQQPVVEPE PVVEETKPAR PPLYYFEEVE
510 520 530 540 550
EKRAREREQL AAWYQPIPEP VKEPEPIKSS LKAPSVAAVP PVEAAAAVSP
560 570 580 590 600
LASGVKKATL ATGAAATVAA PVFSLANSGG PRPQVKEGIG PQLPRPKRIR
610 620 630 640 650
VPTRRELASY GIKLPSQRAA EEKAREAQRN QYDSGDQYND DEIDAMQQDE
660 670 680 690 700
LARQFAQTQQ QRYGEQYQHD VPVNAEDADA AAEAELARQF AQTQQQRYSG
710 720 730 740 750
EQPAGANPFS LDDFEFSPMK ALLDDGPHEP LFTPIVEPVQ QPQQPVAPQQ
760 770 780 790 800
QYQQPQQPVP PQPQYQQPQQ PVAPQPQYQQ PQQPVAPQQQ YQQPQQPVAP
810 820 830 840 850
QQQYQQPQQP VAPQPQDTLL HPLLMRNGDS RPLHKPTTPL PSLDLLTPPP
860 870 880 890 900
SEVEPVDTFA LEQMARLVEA RLADFRIKAD VVNYSPGPVI TRFELNLAPG
910 920 930 940 950
VKAARISNLS RDLARSLSTV AVRVVEVIPG KPYVGLELPN KKRQTVYLRE
960 970 980 990 1000
VLDNAKFRDN PSPLTVVLGK DIAGEPVVAD LAKMPHLLVA GTTGSGKSVG
1010 1020 1030 1040 1050
VNAMILSMLY KAQPEDVRFI MIDPKMLELS VYEGIPHLLT EVVTDMKDAA
1060 1070 1080 1090 1100
NALRWCVNEM ERRYKLMSAL GVRNLAGYNE KIAEADRMMR PIPDPYWKPG
1110 1120 1130 1140 1150
DSMDAQHPVL KKEPYIVVLV DEFADLMMTV GKKVEELIAR LAQKARAAGI
1160 1170 1180 1190 1200
HLVLATQRPS VDVITGLIKA NIPTRIAFTV SSKIDSRTIL DQAGAESLLG
1210 1220 1230 1240 1250
MGDMLYSGPN STLPVRVHGA FVRDQEVHAV VQDWKARGRP QYVDGITSDS
1260 1270 1280 1290 1300
ESEGGAGGFD GAEELDPLFD QAVQFVTEKR KASISGVQRQ FRIGYNRAAR
1310 1320
IIEQMEAQGI VSEQGHNGNR EVLAPPPFD
Length:1,329
Mass (Da):146,663
Last modified:November 1, 1997 - v2
Checksum:iED24BFB464481CFC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti333 – 3342WA → CV in CAA90178 (PubMed:7592387).Curated
Sequence conflicti388 – 3892QP → HA in CAA90178 (PubMed:7592387).Curated
Sequence conflicti1101 – 11033DSM → GQY in CAA90178 (PubMed:7592387).Curated
Sequence conflicti1193 – 11931A → R in CAA90178 (PubMed:7592387).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49932 Genomic DNA. Translation: CAA90178.1.
U00096 Genomic DNA. Translation: AAC73976.1.
AP009048 Genomic DNA. Translation: BAA35615.1.
PIRiA64828.
RefSeqiNP_415410.1. NC_000913.3.
WP_000076967.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73976; AAC73976; b0890.
BAA35615; BAA35615; BAA35615.
GeneIDi945102.
KEGGiecj:JW0873.
eco:b0890.
PATRICi32116991. VBIEscCol129921_0920.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49932 Genomic DNA. Translation: CAA90178.1.
U00096 Genomic DNA. Translation: AAC73976.1.
AP009048 Genomic DNA. Translation: BAA35615.1.
PIRiA64828.
RefSeqiNP_415410.1. NC_000913.3.
WP_000076967.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IUSX-ray2.70A/B/C/D/E/F818-1329[»]
2J5PNMR-A1261-1329[»]
ProteinModelPortaliP46889.
SMRiP46889. Positions 840-1248, 1261-1329.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260652. 426 interactions.
DIPiDIP-9703N.
IntActiP46889. 7 interactions.
MINTiMINT-1261773.
STRINGi511145.b0890.

Protein family/group databases

TCDBi3.A.12.1.2. the septal dna translocator (s-dna-t) family.

Proteomic databases

PaxDbiP46889.
PRIDEiP46889.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73976; AAC73976; b0890.
BAA35615; BAA35615; BAA35615.
GeneIDi945102.
KEGGiecj:JW0873.
eco:b0890.
PATRICi32116991. VBIEscCol129921_0920.

Organism-specific databases

EchoBASEiEB3016.
EcoGeneiEG13226. ftsK.

Phylogenomic databases

eggNOGiENOG4105CNU. Bacteria.
COG1674. LUCA.
HOGENOMiHOG000010001.
InParanoidiP46889.
KOiK03466.
OMAiDPFWKPG.
OrthoDBiEOG6S52GD.

Enzyme and pathway databases

BioCyciEcoCyc:G6464-MONOMER.
ECOL316407:JW0873-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP46889.
PROiP46889.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR025199. FtsK_4TM.
IPR002543. FtsK_dom.
IPR018541. Ftsk_gamma.
IPR027417. P-loop_NTPase.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF13491. FtsK_4TM. 1 hit.
PF09397. Ftsk_gamma. 1 hit.
PF01580. FtsK_SpoIIIE. 1 hit.
[Graphical view]
SMARTiSM00843. Ftsk_gamma. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50901. FTSK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A new Escherichia coli cell division gene, ftsK."
    Begg K.J., Dewar S.J., Donachie W.D.
    J. Bacteriol. 177:6211-6222(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTANT TOE44.
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Role of the C terminus of FtsK in Escherichia coli chromosome segregation."
    Yu X.C., Weihe E.K., Margolin W.
    J. Bacteriol. 180:6424-6428(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CHROMOSOME SEGREGATION, DOMAIN.
  6. "FtsK is an essential cell division protein that is localized to the septum and induced as part of the SOS response."
    Wang L., Lutkenhaus J.
    Mol. Microbiol. 29:731-740(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL DIVISION, SUBCELLULAR LOCATION, INDUCTION.
    Strain: K12.
  7. "Membrane topology of the N-terminus of the Escherichia coli FtsK division protein."
    Dorazi R., Dewar S.J.
    FEBS Lett. 478:13-18(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLU-58, TOPOLOGY.
  8. "FtsQ, FtsL and FtsI require FtsK, but not FtsN, for co-localization with FtsZ during Escherichia coli cell division."
    Chen J.C., Beckwith J.
    Mol. Microbiol. 42:395-413(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. "ZipA is required for recruitment of FtsK, FtsQ, FtsL, and FtsN to the septal ring in Escherichia coli."
    Hale C.A., de Boer P.A.J.
    J. Bacteriol. 184:2552-2556(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. "FtsK is a DNA motor protein that activates chromosome dimer resolution by switching the catalytic state of the XerC and XerD recombinases."
    Aussel L., Barre F.-X., Aroyo M., Stasiak A., Stasiak A.Z., Sherratt D.J.
    Cell 108:195-205(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, HEXAMERIZATION, FUNCTION IN REGULATION OF XERC AND XERD.
  11. "FtsK activities in Xer recombination, DNA mobilization and cell division involve overlapping and separate domains of the protein."
    Bigot S., Corre J., Louarn J.M., Cornet F., Barre F.X.
    Mol. Microbiol. 54:876-886(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN, MUTAGENESIS OF LYS-997.
  12. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: K12 / MG1655 / ATCC 47076.
  13. "Dissection of a functional interaction between the DNA translocase, FtsK, and the XerD recombinase."
    Yates J., Zhekov I., Baker R., Eklund B., Sherratt D.J., Arciszewska L.K.
    Mol. Microbiol. 59:1754-1766(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN, INTERACTION WITH XERD.
    Strain: K12 / AB1157.
  14. "Three functional subdomains of the Escherichia coli FtsQ protein are involved in its interaction with the other division proteins."
    D'Ulisse V., Fagioli M., Ghelardini P., Paolozzi L.
    Microbiology 153:124-138(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FTSQ.
    Strain: K12.
  15. Cited for: REVIEW.
  16. "The Escherichia coli FtsK functional domains involved in its interaction with its divisome protein partners."
    Grenga L., Luzi G., Paolozzi L., Ghelardini P.
    FEMS Microbiol. Lett. 287:163-167(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FTSZ; FTSQ; FTSL AND FTSI.
    Strain: K12.
  17. "Delayed activation of Xer recombination at dif by FtsK during septum assembly in Escherichia coli."
    Kennedy S.P., Chevalier F., Barre F.X.
    Mol. Microbiol. 68:1018-1028(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "Asymmetric DNA requirements in Xer recombination activation by FtsK."
    Bonne L., Bigot S., Chevalier F., Allemand J.F., Barre F.X.
    Nucleic Acids Res. 37:2371-2380(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN.
  19. "Multiple regions along the Escherichia coli FtsK protein are implicated in cell division."
    Dubarry N., Possoz C., Barre F.X.
    Mol. Microbiol. 78:1088-1100(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.
    Strain: K12 / AB1157.
  20. Cited for: FUNCTION.
  21. "DNA chirality-dependent stimulation of topoisomerase IV activity by the C-terminal AAA+ domain of FtsK."
    Bigot S., Marians K.J.
    Nucleic Acids Res. 38:3031-3040(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  22. Cited for: REVIEW.
  23. "FtsK DNA translocase: the fast motor that knows where it's going."
    Crozat E., Grainge I.
    ChemBioChem 11:2232-2243(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  24. "Activation of XerCD-dif recombination by the FtsK DNA translocase."
    Grainge I., Lesterlin C., Sherratt D.J.
    Nucleic Acids Res. 39:5140-5148(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN.
  25. "Site-directed fluorescence labeling reveals a revised N-terminal membrane topology and functional periplasmic residues in the Escherichia coli cell division protein FtsK."
    Berezuk A.M., Goodyear M., Khursigara C.M.
    J. Biol. Chem. 289:23287-23301(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF ASP-135; ASP-136; ILE-137 AND TRP-138.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  26. "Double-stranded DNA translocation: structure and mechanism of hexameric FtsK."
    Massey T.H., Mercogliano C.P., Yates J., Sherratt D.J., Lowe J.
    Mol. Cell 23:457-469(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 818-1329, SUBUNIT.
  27. Cited for: STRUCTURE BY NMR OF 1261-1329, DNA-BINDING.

Entry informationi

Entry nameiFTSK_ECOLI
AccessioniPrimary (citable) accession number: P46889
Secondary accession number(s): P77450
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1997
Last modified: April 13, 2016
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.