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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)DescriptionActionsGraphical viewLength
Nucleotide bindingi994 – 999ATPPROSITE-ProRule annotation6

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13226. ftsK.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 24Cytoplasmic1 PublicationAdd BLAST24
Transmembranei25 – 44Helical1 PublicationAdd BLAST20
Topological domaini45 – 74Periplasmic1 PublicationAdd BLAST30
Transmembranei75 – 98Helical1 PublicationAdd BLAST24
Topological domaini99 – 115Cytoplasmic1 PublicationAdd BLAST17
Transmembranei116 – 132Helical1 PublicationAdd BLAST17
Topological domaini133 – 162Periplasmic1 PublicationAdd BLAST30
Transmembranei163 – 179Helical1 PublicationAdd BLAST17
Topological domaini180 – 1329Cytoplasmic1 PublicationAdd BLAST1150

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)DescriptionActionsGraphical viewLength
Mutagenesisi58E → A: Loss of function. 1 Publication1
Mutagenesisi80G → A in Toe44; loss of function under extreme conditions. 1
Mutagenesisi135D → 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 Publication1
Mutagenesisi136D → 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 Publication1
Mutagenesisi137I → 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 Publication1
Mutagenesisi138W → 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 Publication1
Mutagenesisi997K → A: Does not activate Xer recombination. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000982571 – 1329DNA translocase FtsKAdd BLAST1329

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 interactors.
DIPiDIP-9703N.
IntActiP46889. 7 interactors.
MINTiMINT-1261773.
STRINGi511145.b0890.

Structurei

Secondary structure

11329
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi843 – 845Combined sources3
Helixi859 – 872Combined sources14
Turni873 – 876Combined sources4
Beta strandi879 – 886Combined sources8
Beta strandi888 – 897Combined sources10
Helixi904 – 907Combined sources4
Helixi910 – 916Combined sources7
Beta strandi923 – 926Combined sources4
Beta strandi931 – 939Combined sources9
Helixi948 – 952Combined sources5
Helixi955 – 958Combined sources4
Beta strandi965 – 971Combined sources7
Beta strandi976 – 980Combined sources5
Helixi981 – 983Combined sources3
Beta strandi986 – 990Combined sources5
Helixi997 – 1009Combined sources13
Turni1014 – 1016Combined sources3
Beta strandi1017 – 1022Combined sources6
Beta strandi1025 – 1027Combined sources3
Helixi1028 – 1032Combined sources5
Beta strandi1038 – 1041Combined sources4
Helixi1046 – 1069Combined sources24
Helixi1075 – 1087Combined sources13
Beta strandi1115 – 1121Combined sources7
Helixi1123 – 1144Combined sources22
Helixi1146 – 1148Combined sources3
Beta strandi1150 – 1157Combined sources8
Turni1161 – 1163Combined sources3
Helixi1166 – 1171Combined sources6
Beta strandi1174 – 1178Combined sources5
Helixi1183 – 1190Combined sources8
Beta strandi1191 – 1193Combined sources3
Helixi1195 – 1197Combined sources3
Beta strandi1203 – 1207Combined sources5
Beta strandi1215 – 1219Combined sources5
Helixi1224 – 1235Combined sources12
Turni1262 – 1264Combined sources3
Helixi1269 – 1279Combined sources11
Beta strandi1281 – 1283Combined sources3
Helixi1284 – 1290Combined sources7
Helixi1295 – 1308Combined sources14
Beta strandi1316 – 1322Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IUSX-ray2.70A/B/C/D/E/F818-1329[»]
2J5PNMR-A1261-1329[»]
5DCFX-ray2.30A1261-1329[»]
ProteinModelPortaliP46889.
SMRiP46889.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46889.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini974 – 1187FtsKPROSITE-ProRule annotationAdd BLAST214

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni184 – 817LinkerAdd BLAST634
Regioni818 – 943AlphaAdd BLAST126
Regioni944 – 1258BetaAdd BLAST315
Regioni1259 – 1329GammaAdd BLAST71

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi331 – 822Gln/Glu/Pro-richAdd BLAST492

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.

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)DescriptionActionsGraphical viewLength
Sequence conflicti333 – 334WA → CV in CAA90178 (PubMed:7592387).Curated2
Sequence conflicti388 – 389QP → HA in CAA90178 (PubMed:7592387).Curated2
Sequence conflicti1101 – 1103DSM → GQY in CAA90178 (PubMed:7592387).Curated3
Sequence conflicti1193A → R in CAA90178 (PubMed:7592387).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IUSX-ray2.70A/B/C/D/E/F818-1329[»]
2J5PNMR-A1261-1329[»]
5DCFX-ray2.30A1261-1329[»]
ProteinModelPortaliP46889.
SMRiP46889.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260652. 426 interactors.
DIPiDIP-9703N.
IntActiP46889. 7 interactors.
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.

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...

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: November 30, 2016
This is version 146 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.