P46889 (FTSK_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA translocase FtsK

Gene names

Name:	ftsK
Ordered Locus Names:	b0890, JW0873

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	1329 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.5 Ref.6 Ref.8 Ref.10 Ref.11 Ref.13 Ref.17 Ref.18 Ref.20 Ref.21 Ref.24
Subunit structure	Homohexamer. Forms a ring that surrounds DNA. Interacts with FtsZ, FtsQ, FtsL and FtsI. Ref.10 Ref.13 Ref.14 Ref.16 Ref.25
Subcellular location	Cell inner membrane; Multi-pass membrane protein. Note: Located at the septum. Colocalizes with FtsZ. ZipA, FtsZ and FtsA, but not FtsI and FtsQ are required to target it to the septum. Ref.6 Ref.8 Ref.9 Ref.12
Induction	Induced by DNA-damaging agents. Ref.6
Domain	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. Ref.5 Ref.11 Ref.13 Ref.18 Ref.19 Ref.24
Sequence similarities	Belongs to the FtsK/SpoIIIE/SftA family. Contains 1 FtsK domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Chromosome partition
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding DNA-binding Nucleotide-binding
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cellular response to antibiotic Inferred from mutant phenotype Ref.6. Source: EcoliWiki chromosome segregation Inferred from direct assay Ref.20. Source: EcoliWiki cytokinetic cell separation Inferred from mutant phenotype PubMed 9294448. Source: EcoliWiki positive regulation of catalytic activity Inferred from direct assay Ref.24. Source: EcoCyc positive regulation of transcription, DNA-dependent Inferred from mutant phenotype PubMed 9294448. Source: EcoliWiki response to salt stress Inferred from mutant phenotype PubMed 9294448. Source: EcoliWiki
Cellular_component	integral to plasma membrane Inferred from direct assay Ref.7. Source: EcoCyc
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA translocase activity Inferred from direct assay PubMed 16301526Ref.18. Source: EcoCyc sequence-specific DNA binding Inferred from direct assay Ref.26. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ftsQ	P06136	3	EBI-550795,EBI-1130157

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1329

1329

DNA translocase FtsK

PRO_0000098257

Regions

Transmembrane

22 – 42

21

Helical; Potential

Transmembrane

76 – 96

21

Helical; Potential

Transmembrane

112 – 132

21

Helical; Potential

Transmembrane

137 – 157

21

Helical; Potential

Transmembrane

164 – 184

21

Helical; Potential

Topological domain

185 – 1329

1145

Cytoplasmic Potential

Domain

974 – 1187

214

FtsK

Nucleotide binding

994 – 999

6

ATP By similarity

Region

184 – 817

634

Linker

Region

818 – 943

126

Alpha

Region

944 – 1258

315

Beta

Region

1259 – 1329

71

Gamma

Compositional bias

331 – 822

492

Gln/Glu/Pro-rich

Experimental info

Mutagenesis

58

1

E → A: Loss of function. Ref.7

Mutagenesis

80

1

G → A in Toe44; loss of function under extreme conditions.

Mutagenesis

997

1

K → A: Does not activate Xer recombination. Ref.11

Sequence conflict

333 – 334

2

WA → CV in CAA90178. Ref.1

Sequence conflict

388 – 389

2

QP → HA in CAA90178. Ref.1

Sequence conflict

1101 – 1103

3

DSM → GQY in CAA90178. Ref.1

Sequence conflict

1193

1

A → R in CAA90178. Ref.1

Secondary structure

1

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1329

Helix Strand Turn

Details...

Helix

843 – 845

3

Helix

859 – 872

14

Turn

873 – 876

4

Beta strand

879 – 886

8

Beta strand

888 – 897

10

Helix

904 – 907

4

Helix

910 – 916

7

Beta strand

923 – 926

4

Beta strand

931 – 939

9

Helix

948 – 952

5

Helix

955 – 958

4

Beta strand

965 – 971

7

Beta strand

976 – 980

5

Helix

981 – 983

3

Beta strand

986 – 990

5

Helix

997 – 1009

13

Turn

1014 – 1016

3

Beta strand

1017 – 1022

6

Beta strand

1025 – 1027

3

Helix

1028 – 1032

5

Beta strand

1038 – 1041

4

Helix

1046 – 1069

24

Helix

1075 – 1087

13

Beta strand

1115 – 1121

7

Helix

1123 – 1144

22

Helix

1146 – 1148

3

Beta strand

1150 – 1157

8

Turn

1161 – 1163

3

Helix

1166 – 1171

6

Beta strand

1174 – 1178

5

Helix

1183 – 1190

8

Beta strand

1191 – 1193

3

Helix

1195 – 1197

3

Beta strand

1203 – 1207

5

Beta strand

1215 – 1219

5

Helix

1224 – 1235

12

Turn

1262 – 1264

3

Helix

1269 – 1278

10

Beta strand

1281 – 1283

3

Helix

1284 – 1291

8

Helix

1295 – 1308

14

Beta strand

1316 – 1322

7

Sequences

	Sequence		Length	Mass (Da)
	P46889 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: ED24BFB464481CFC	FASTA	1,329	146,663
	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

References

	« Hide 'large scale' referencesShow '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] [Europe PMC] [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. , 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] [Europe PMC] [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] [Europe PMC] [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] [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]	"FtsK, a literate chromosome segregation machine." Bigot S., Sivanathan V., Possoz C., Barre F.X., Cornet F. Mol. Microbiol. 64:1434-1441(2007) [PubMed] [Europe PMC] [Abstract] 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]	"FtsK translocation on DNA stops at XerCD-dif." Graham J.E., Sivanathan V., Sherratt D.J., Arciszewska L.K. Nucleic Acids Res. 38:72-81(2010) [PubMed] [Europe PMC] [Abstract] 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]	"The Escherichia coli DNA translocase FtsK." Sherratt D.J., Arciszewska L.K., Crozat E., Graham J.E., Grainge I. Biochem. Soc. Trans. 38:395-398(2010) [PubMed] [Europe PMC] [Abstract] 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]	"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.
[26]	"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] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1261-1329, DNA-BINDING.
+	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.

PIR

A64828.

RefSeq

NP_415410.1. NC_000913.2.
YP_489162.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IUS	X-ray	2.70	A/B/C/D/E/F	818-1329	[»]
2J5P	NMR	-	A	1261-1329	[»]

ProteinModelPortal

P46889.

SMR

P46889. Positions 840-1248, 1261-1329.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9703N.

IntAct

P46889. 7 interactions.

MINT

MINT-1261773.

STRING

511145.b0890.

Protein family/group databases

TCDB

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

Proteomic databases

PaxDb

P46889.

PRIDE

P46889.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73976; AAC73976; b0890.
BAA35615; BAA35615; BAA35615.

GeneID

12931658.
945102.

KEGG

ecj:Y75_p0862.
eco:b0890.

PATRIC

32116991. VBIEscCol129921_0920.

Organism-specific databases

EchoBASE

EB3016.

EcoGene

EG13226. ftsK.

Phylogenomic databases

eggNOG

COG1674.

HOGENOM

HOG000010001.

KO

K03466.

OMA

YQPEPAP.

ProtClustDB

PRK10263.

Enzyme and pathway databases

BioCyc

EcoCyc:G6464-MONOMER.
ECOL316407:JW0873-MONOMER.

Gene expression databases

Genevestigator

P46889.

Family and domain databases

InterPro

IPR002543. Cell_div_FtsK/SpoIIIE.
IPR018541. DNA_translocase_Ftsk_gamma.
IPR025199. DUF4117.
[Graphical view]

Pfam

PF13491. DUF4117. 1 hit.
PF09397. Ftsk_gamma. 1 hit.
PF01580. FtsK_SpoIIIE. 1 hit.
[Graphical view]

SMART

SM00843. Ftsk_gamma. 1 hit.
[Graphical view]

PROSITE

PS50901. FTSK. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P46889.

Entry information

Entry name

FTSK_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program