Reviewed, UniProtKB/Swiss-Prot P46889 (FTSK_ECOLI)

Names and origin

Protein names

Recommended name:
    DNA translocase ftsK

Gene names

Name:	ftsK
Ordered Locus Names:	b0890, JW0873

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	1329 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Cell cycle Cell division Chromosome partition
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane
Ligand	ATP-binding DNA-binding Nucleotide-binding
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW chromosome segregation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
aceE	P0AFG8	1	EBI-550795,EBI-542683

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 – 44

23

Potential

Transmembrane

75 – 97

23

Potential

Transmembrane

110 – 132

23

Potential

Transmembrane

137 – 158

22

Potential

Transmembrane

165 – 187

23

Potential

Domain

974 – 1187

214

FtsK

Nucleotide binding

991 – 998

8

ATP Potential

Region

1 – 202

202

N-terminus

Region

179 – 230

52

Hexamerization

Compositional bias

331 – 822

492

Gln/Glu/Pro-rich

Experimental info

Mutagenesis

58

1

E → A: Loss of function. Ref.5

Mutagenesis

80

1

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

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)
	P46889-1 [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: 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. , 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.

Cross-references

Sequence databases

EMBLGenBankDDBJ

Z49932 Genomic DNA. Translation: CAA90178.1.
U00096 Genomic DNA. Translation: AAC73976.1.
AP009048 Genomic DNA. Translation: BAA35615.1.

PIR

A64828.

RefSeq

AP_001520.1.
NP_415410.1.

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:9703N.

IntAct

P46889. 5 interactions.

Protein family/group databases

TCDB

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

Genome annotation databases

GeneID

945102.

GenomeReviews

Gene locus JW0873 in contig AP009048_GR.
Gene locus b0890 in contig U00096_GR.

KEGG

ecj:JW0873.
eco:b0890.

Organism-specific databases

EchoBASE

EB3016.

EcoGene

EG13226. ftsK.

CMR

Search...

Phylogenomic databases

HOGENOM

P46889.

OMA

P46889. EQPVQQP.

Enzyme and pathway databases

BioCyc

EcoCyc:G6464-MON.

Family and domain databases

InterPro

IPR018541. DNA_translocase_Ftsk_gamma.
IPR002543. FtsK_SpoIIIE.
[Graphical view]

Pfam

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

PROSITE

PS50901. FTSK. 1 hit.
[Graphical view]

ProtoNet

Search...

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:	June 16, 2009
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)