Skip Header

Contribute Send feedback
Read comments (?) or add your own

P46889 (FTSK_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA translocase FtsK
Gene names
Name:ftsK
Ordered Locus Names:b0890, JW0873
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length1329 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

DNA motor protein, which is both required to move DNA out of the region of the septum during cell division and for the septum formation. Tracks DNA in an ATP-dependent manner by generating positive supercoils in front of it and negative supercoils behind it. Also plays a role in resolution of dimer chromosomes by regulating the XerC and XerD recombination complex, possibly by switching the catalytic state of the two recombinases. Required for the targeting of FtsQ, FtsL and FtsI to the septum. Ref.6 Ref.8

Subunit structure

Homohexamer. This suggests the formation of a ring between the two cells at the septum that surrounds DNA. Ref.8

Subcellular location

Cell inner membrane; Multi-pass membrane protein; Cytoplasmic side. Note: Located at the septum. The large C-terminal part of the protein is cytoplasmic. Colocalizes with FtsZ. ZipA is required to target it to the septum. Ref.6 Ref.7 Ref.9

Domain

The N-terminus domain is sufficient for the localization to the septal ring.

The hexamerization domain is required for the formation of a homohexamer, suggesting the formation of a ring between the two cells that surrounds DNA.

Sequence similarities

Contains 1 FtsK domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

aceEP0AFG81EBI-550795,EBI-542683

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13291329DNA translocase FtsK
PRO_0000098257

Regions

Transmembrane22 – 4423Helical; Potential
Transmembrane75 – 9723Helical; Potential
Transmembrane110 – 13223Helical; Potential
Transmembrane137 – 15822Helical; Potential
Transmembrane165 – 18723Helical; Potential
Domain974 – 1187214FtsK
Nucleotide binding991 – 9988ATP Potential
Region1 – 202202N-terminus
Region179 – 23052Hexamerization
Compositional bias331 – 822492Gln/Glu/Pro-rich

Experimental info

Mutagenesis581E → A: Loss of function. Ref.5
Mutagenesis801G → A in Toe44; loss of function under extreme conditions.
Sequence conflict333 – 3342WA → CV in CAA90178. Ref.1
Sequence conflict388 – 3892QP → HA in CAA90178. Ref.1
Sequence conflict1101 – 11033DSM → GQY in CAA90178. Ref.1
Sequence conflict11931A → R in CAA90178. Ref.1

Secondary structure

............................................................................... 1329
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P46889 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: ED24BFB464481CFC

FASTA1,329146,663
        10         20         30         40         50         60 
MSQEYIEDKE VTLTKLSSGR RLLEALLILI VLFAVWLMAA LLSFNPSDPS WSQTAWHEPI 

        70         80         90        100        110        120 
HNLGGMPGAW LADTLFFIFG VMAYTIPVII VGGCWFAWRH QSSDEYIDYF AVSLRIIGVL 

       130        140        150        160        170        180 
ALILTSCGLA AINADDIWYF ASGGVIGSLL STTLQPLLHS SGGTIALLCV WAAGLTLFTG 

       190        200        210        220        230        240 
WSWVTIAEKL GGWILNILTF ASNRTRRDDT WVDEDEYEDD EEYEDENHGK QHESRRARIL 

       250        260        270        280        290        300 
RGALARRKRL AEKFINPMGR QTDAALFSGK RMDDDEEITY TARGVAADPD DVLFSGNRAT 

       310        320        330        340        350        360 
QPEYDEYDPL LNGAPITEPV AVAAAATTAT QSWAAPVEPV TQTPPVASVD VPPAQPTVAW 

       370        380        390        400        410        420 
QPVPGPQTGE PVIAPAPEGY PQQSQYAQPA VQYNEPLQQP VQPQQPYYAP AAEQPAQQPY 

       430        440        450        460        470        480 
YAPAPEQPVA GNAWQAEEQQ STFAPQSTYQ TEQTYQQPAA QEPLYQQPQP VEQQPVVEPE 

       490        500        510        520        530        540 
PVVEETKPAR PPLYYFEEVE EKRAREREQL AAWYQPIPEP VKEPEPIKSS LKAPSVAAVP 

       550        560        570        580        590        600 
PVEAAAAVSP LASGVKKATL ATGAAATVAA PVFSLANSGG PRPQVKEGIG PQLPRPKRIR 

       610        620        630        640        650        660 
VPTRRELASY GIKLPSQRAA EEKAREAQRN QYDSGDQYND DEIDAMQQDE LARQFAQTQQ 

       670        680        690        700        710        720 
QRYGEQYQHD VPVNAEDADA AAEAELARQF AQTQQQRYSG EQPAGANPFS LDDFEFSPMK 

       730        740        750        760        770        780 
ALLDDGPHEP LFTPIVEPVQ QPQQPVAPQQ QYQQPQQPVP PQPQYQQPQQ PVAPQPQYQQ 

       790        800        810        820        830        840 
PQQPVAPQQQ YQQPQQPVAP QQQYQQPQQP VAPQPQDTLL HPLLMRNGDS RPLHKPTTPL 

       850        860        870        880        890        900 
PSLDLLTPPP SEVEPVDTFA LEQMARLVEA RLADFRIKAD VVNYSPGPVI TRFELNLAPG 

       910        920        930        940        950        960 
VKAARISNLS RDLARSLSTV AVRVVEVIPG KPYVGLELPN KKRQTVYLRE VLDNAKFRDN 

       970        980        990       1000       1010       1020 
PSPLTVVLGK DIAGEPVVAD LAKMPHLLVA GTTGSGKSVG VNAMILSMLY KAQPEDVRFI 

      1030       1040       1050       1060       1070       1080 
MIDPKMLELS VYEGIPHLLT EVVTDMKDAA NALRWCVNEM ERRYKLMSAL GVRNLAGYNE 

      1090       1100       1110       1120       1130       1140 
KIAEADRMMR PIPDPYWKPG DSMDAQHPVL KKEPYIVVLV DEFADLMMTV GKKVEELIAR 

      1150       1160       1170       1180       1190       1200 
LAQKARAAGI HLVLATQRPS VDVITGLIKA NIPTRIAFTV SSKIDSRTIL DQAGAESLLG 

      1210       1220       1230       1240       1250       1260 
MGDMLYSGPN STLPVRVHGA FVRDQEVHAV VQDWKARGRP QYVDGITSDS ESEGGAGGFD 

      1270       1280       1290       1300       1310       1320 
GAEELDPLFD QAVQFVTEKR KASISGVQRQ FRIGYNRAAR IIEQMEAQGI VSEQGHNGNR 


EVLAPPPFD 

« Hide

References

« Hide 'large scale' references
[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: 7592387] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTANT TOE44.
Strain: K12.
[2]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
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: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"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: 10922461] [Abstract]
Cited for: MUTAGENESIS OF GLU-58.
[6]"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: 11703663] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]"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: 11948172] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"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: 11832210] [Abstract]
Cited for: FUNCTION, HEXAMERIZATION, REGULATION OF XERC AND XERD.
[9]"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: 15919996] [Abstract]
Cited for: SUBCELLULAR LOCATION.
Strain: K12 / MG1655 / ATCC 47076.
[10]"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: 16916635] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 818-1329.
[11]"The FtsK gamma domain directs oriented DNA translocation by interacting with KOPS."
Sivanathan V., Allen M.D., de Bekker C., Baker R., Arciszewska L.K., Freund S.M., Bycroft M., Lowe J., Sherratt D.J.
Nat. Struct. Mol. Biol. 13:965-972(2006) [PubMed: 17057717] [Abstract]
Cited for: STRUCTURE BY NMR OF 1261-1329.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z49932 Genomic DNA. Translation: CAA90178.1.
U00096 Genomic DNA. Translation: AAC73976.1.
AP009048 Genomic DNA. Translation: BAA35615.1.
PIRA64828.
RefSeqNP_415410.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IUSX-ray2.70A/B/C/D/E/F818-1329[»]
2J5PNMR-A1261-1329[»]
ProteinModelPortalP46889.
SMRP46889. Positions 840-1248, 1261-1329.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-9703N.
IntActP46889. 5 interactions.
MINTMINT-1261773.

Protein family/group databases

TCDB3.A.12.1.2. septal DNA translocator (S-DNA-T) family.

Proteomic databases

PRIDEP46889.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000000548; EBESCP00000000548; EBESCG00000000460.
EBESCT00000000549; EBESCP00000000549; EBESCG00000000460.
EBESCT00000000550; EBESCP00000000550; EBESCG00000000460.
EBESCT00000018339; EBESCP00000017630; EBESCG00000017393.
GeneID945102.
GenomeReviewsGene locus JW0873 in contig AP009048_GR.
Gene locus b0890 in contig U00096_GR.
KEGGecj:JW0873.
eco:b0890.
PATRIC32116991. VBIEscCol129921_0920.

Organism-specific databases

EchoBASEEB3016.
EcoGeneEG13226. ftsK.

Phylogenomic databases

eggNOGCOG1674.
GeneTreeEBGT00050000008749.
HOGENOMHBG662140.
OMAYQPEPAP.
PhylomeDBP46889.
ProtClustDBPRK10263.

Enzyme and pathway databases

BioCycEcoCyc:G6464-MONOMER.

Gene expression databases

GenevestigatorP46889.

Family and domain databases

InterProIPR002543. Cell_div_FtsK/SpoIIIE.
IPR018541. DNA_translocase_Ftsk_gamma.
[Graphical view]
KOK03466.
PfamPF09397. Ftsk_gamma. 1 hit.
PF01580. FtsK_SpoIIIE. 1 hit.
[Graphical view]
SMARTSM00843. Ftsk_gamma. 1 hit.
[Graphical view]
PROSITEPS50901. FTSK. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFTSK_ECOLI
AccessionPrimary (citable) accession number: P46889
Secondary accession number(s): P77450
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1997
Last modified: January 25, 2012
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families