ECOLI:FTSK

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	ftsK
Protein Name(s)	DNA translocase FtsK
External Links
UniProt	P46889
EMBL	Z49932 U00096 AP009048
PIR	A64828
RefSeq	NP_415410.1 YP_489162.1
PDB	2IUS 2J5P
PDBsum	2IUS 2J5P
ProteinModelPortal	P46889
SMR	P46889
DIP	DIP-9703N
IntAct	P46889
MINT	MINT-1261773
STRING	511145.b0890
TCDB	3.A.12.1.2
PaxDb	P46889
PRIDE	P46889
EnsemblBacteria	AAC73976 BAA35615
GeneID	12931658 945102
KEGG	ecj:Y75_p0862 eco:b0890
PATRIC	32116991
EchoBASE	EB3016
EcoGene	EG13226
eggNOG	COG1674
HOGENOM	HOG000010001
InParanoid	P46889
KO	K03466
OMA	DPFWKPG
OrthoDB	EOG6S52GD
BioCyc	EcoCyc:G6464-MONOMER ECOL316407:JW0873-MONOMER
EvolutionaryTrace	P46889
PRO	PR:P46889
Proteomes	UP000000318 UP000000625
Genevestigator	P46889
GO	GO:0005887 GO:0016020 GO:0005886 GO:0005524 GO:0016887 GO:0003677 GO:0015616 GO:0033676 GO:0042802 GO:0043565 GO:0006200 GO:0051301 GO:0071236 GO:0007059 GO:0000920 GO:0043085 GO:0045893 GO:0006970 GO:0009651
Gene3D	3.40.50.300
InterPro	IPR025199 IPR002543 IPR018541 IPR027417
Pfam	PF13491 PF09397 PF01580
SMART	SM00843
SUPFAM	SSF52540
PROSITE	PS50901

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0051301	cell division	PMID:21091498^[1]	ECO:0000315			P	As shown in figure 5, cells with a deletion mutation of varying parts of FtsK form elongate rods, which is indicative of the cell's inability to divide.	complete CACAO 6611
	GO:0016887	ATPase activity	PMID:20081205^[2]	ECO:0000314			F	As indicated in figure 5, ATP is hydrolyzed at a significantly greater rate when FtsK is introduced.	complete CACAO 6620
	GO:0033676	double-stranded DNA-dependent ATPase activity	PMID:16916635^[3]	ECO:0000315			F	As shown in figure 1C, wild type FtsK shows significant DNA-dependent ATPase activity in comparison to FtsK containing a mutation in the walker A motif, which sees significantly inhibited activity.	complete CACAO 6781
involved_in	GO:0051301	cell division	PMID:21091498^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0033676	double-stranded DNA-dependent ATPase activity	PMID:16916635^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	PMID:20081205^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0071236	cellular response to antibiotic	PMID:9723913^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0051301	cell division	PMID:9829960^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0051301	cell division	PMID:9721304^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0051301	cell division	PMID:9294448^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0051301	cell division	PMID:7592387^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045893	positive regulation of transcription, DNA-templated	PMID:9294448^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	PMID:19854947^[9]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	PMID:18722176^[10]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:9723913^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:10922461^[11]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0015616	DNA translocase activity	PMID:19854947^[9]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0009651	response to salt stress	PMID:9294448^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007059	chromosome segregation	PMID:19854947^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0A8P6 UniProtKB:P0A8P8	P	Seeded From UniProt	complete
involved_in	GO:0007059	chromosome segregation	PMID:12034757^[12]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P0A734 UniProtKB:P0AEZ3 UniProtKB:P18196	P	Seeded From UniProt	complete
involved_in	GO:0007059	chromosome segregation	PMID:9829960^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007059	chromosome segregation	PMID:17805344^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007059	chromosome segregation	PMID:12034757^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007059	chromosome segregation	PMID:19854947^[9]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006970	response to osmotic stress	PMID:9294448^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:10922461^[11]	ECO:0000269	experimental evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:18722176^[10]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0000920	septum digestion after cytokinesis	PMID:9294448^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0043565	sequence-specific DNA binding	PMID:17041598^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0043565	sequence-specific DNA binding	PMID:17057717^[15]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0043085	positive regulation of catalytic activity	PMID:21371996^[16]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:24302254^[17]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0015616	DNA translocase activity	PMID:19246541^[18]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0015616	DNA translocase activity	PMID:16301526^[19]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005887	integral component of plasma membrane	PMID:10922461^[11]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:15919996^[20]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002543	F	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002543	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002543	F	Seeded From UniProt	complete
involved_in	GO:0051301	cell division	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0132	P	Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F	Seeded From UniProt	complete
involved_in	GO:0007059	chromosome segregation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0159	P	Seeded From UniProt	complete
involved_in	GO:0007049	cell cycle	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0131	P	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003 UniProtKB-KW:KW-0997 UniProtKB-SubCell:SL-0037	C	Seeded From UniProt	complete
part_of	GO:0016021	integral component of membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0812	C	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0238	F	Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Dubarry, N et al. (2010) Multiple regions along the Escherichia coli FtsK protein are implicated in cell division. Mol. Microbiol. 78 1088-100 PubMed GONUTS page
↑ ^2.0 ^2.1 Bigot, S & Marians, KJ (2010) DNA chirality-dependent stimulation of topoisomerase IV activity by the C-terminal AAA+ domain of FtsK. Nucleic Acids Res. 38 3031-40 PubMed GONUTS page
↑ ^3.0 ^3.1 Massey, TH et al. (2006) Double-stranded DNA translocation: structure and mechanism of hexameric FtsK. Mol. Cell 23 457-69 PubMed GONUTS page
↑ ^4.0 ^4.1 Wang, L & Lutkenhaus, J (1998) FtsK is an essential cell division protein that is localized to the septum and induced as part of the SOS response. Mol. Microbiol. 29 731-40 PubMed GONUTS page
↑ ^5.0 ^5.1 Yu, XC et al. (1998) Role of the C terminus of FtsK in Escherichia coli chromosome segregation. J. Bacteriol. 180 6424-8 PubMed GONUTS page
↑ Draper, GC et al. (1998) Only the N-terminal domain of FtsK functions in cell division. J. Bacteriol. 180 4621-7 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 ^7.4 Diez, AA et al. (1997) A mutation in the ftsK gene of Escherichia coli affects cell-cell separation, stationary-phase survival, stress adaptation, and expression of the gene encoding the stress protein UspA. J. Bacteriol. 179 5878-83 PubMed GONUTS page
↑ Begg, KJ et al. (1995) A new Escherichia coli cell division gene, ftsK. J. Bacteriol. 177 6211-22 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 ^9.3 Graham, JE et al. (2010) FtsK translocation on DNA stops at XerCD-dif. Nucleic Acids Res. 38 72-81 PubMed GONUTS page
↑ ^10.0 ^10.1 Löwe, J et al. (2008) Molecular mechanism of sequence-directed DNA loading and translocation by FtsK. Mol. Cell 31 498-509 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 Dorazi, R & Dewar, SJ (2000) Membrane topology of the N-terminus of the Escherichia coli FtsK division protein. FEBS Lett. 478 13-8 PubMed GONUTS page
↑ ^12.0 ^12.1 Capiaux, H et al. (2002) A dual role for the FtsK protein in Escherichia coli chromosome segregation. EMBO Rep. 3 532-6 PubMed GONUTS page
↑ Grainge, I et al. (2007) Unlinking chromosome catenanes in vivo by site-specific recombination. EMBO J. 26 4228-38 PubMed GONUTS page
↑ Ptacin, JL et al. (2006) Identification of the FtsK sequence-recognition domain. Nat. Struct. Mol. Biol. 13 1023-5 PubMed GONUTS page
↑ Sivanathan, V et al. (2006) The FtsK gamma domain directs oriented DNA translocation by interacting with KOPS. Nat. Struct. Mol. Biol. 13 965-72 PubMed GONUTS page
↑ Grainge, I et al. (2011) Activation of XerCD-dif recombination by the FtsK DNA translocase. Nucleic Acids Res. 39 5140-8 PubMed GONUTS page
↑ Bisicchia, P et al. (2013) The N-terminal membrane-spanning domain of the Escherichia coli DNA translocase FtsK hexamerizes at midcell. MBio 4 e00800-13 PubMed GONUTS page
↑ Bonné, L et al. (2009) Asymmetric DNA requirements in Xer recombination activation by FtsK. Nucleic Acids Res. 37 2371-80 PubMed GONUTS page
↑ Levy, O et al. (2005) Identification of oligonucleotide sequences that direct the movement of the Escherichia coli FtsK translocase. Proc. Natl. Acad. Sci. U.S.A. 102 17618-23 PubMed GONUTS page
↑ Daley, DO et al. (2005) Global topology analysis of the Escherichia coli inner membrane proteome. Science 308 1321-3 PubMed GONUTS page

[PMID:21091498-1] 1.0 ^1.1 Dubarry, N et al. (2010) Multiple regions along the Escherichia coli FtsK protein are implicated in cell division. Mol. Microbiol. 78 1088-100 PubMed GONUTS page

[PMID:20081205-2] 2.0 ^2.1 Bigot, S & Marians, KJ (2010) DNA chirality-dependent stimulation of topoisomerase IV activity by the C-terminal AAA+ domain of FtsK. Nucleic Acids Res. 38 3031-40 PubMed GONUTS page

[PMID:16916635-3] 3.0 ^3.1 Massey, TH et al. (2006) Double-stranded DNA translocation: structure and mechanism of hexameric FtsK. Mol. Cell 23 457-69 PubMed GONUTS page

[PMID:9723913-4] 4.0 ^4.1 Wang, L & Lutkenhaus, J (1998) FtsK is an essential cell division protein that is localized to the septum and induced as part of the SOS response. Mol. Microbiol. 29 731-40 PubMed GONUTS page

[PMID:9829960-5] 5.0 ^5.1 Yu, XC et al. (1998) Role of the C terminus of FtsK in Escherichia coli chromosome segregation. J. Bacteriol. 180 6424-8 PubMed GONUTS page

[PMID:9721304-6] Draper, GC et al. (1998) Only the N-terminal domain of FtsK functions in cell division. J. Bacteriol. 180 4621-7 PubMed GONUTS page

[PMID:9294448-7] 7.0 ^7.1 ^7.2 ^7.3 ^7.4 Diez, AA et al. (1997) A mutation in the ftsK gene of Escherichia coli affects cell-cell separation, stationary-phase survival, stress adaptation, and expression of the gene encoding the stress protein UspA. J. Bacteriol. 179 5878-83 PubMed GONUTS page

[PMID:7592387-8] Begg, KJ et al. (1995) A new Escherichia coli cell division gene, ftsK. J. Bacteriol. 177 6211-22 PubMed GONUTS page

[PMID:19854947-9] 9.0 ^9.1 ^9.2 ^9.3 Graham, JE et al. (2010) FtsK translocation on DNA stops at XerCD-dif. Nucleic Acids Res. 38 72-81 PubMed GONUTS page

[PMID:18722176-10] 10.0 ^10.1 Löwe, J et al. (2008) Molecular mechanism of sequence-directed DNA loading and translocation by FtsK. Mol. Cell 31 498-509 PubMed GONUTS page

[PMID:10922461-11] 11.0 ^11.1 ^11.2 Dorazi, R & Dewar, SJ (2000) Membrane topology of the N-terminus of the Escherichia coli FtsK division protein. FEBS Lett. 478 13-8 PubMed GONUTS page

[PMID:12034757-12] 12.0 ^12.1 Capiaux, H et al. (2002) A dual role for the FtsK protein in Escherichia coli chromosome segregation. EMBO Rep. 3 532-6 PubMed GONUTS page

[PMID:17805344-13] Grainge, I et al. (2007) Unlinking chromosome catenanes in vivo by site-specific recombination. EMBO J. 26 4228-38 PubMed GONUTS page

[PMID:17041598-14] Ptacin, JL et al. (2006) Identification of the FtsK sequence-recognition domain. Nat. Struct. Mol. Biol. 13 1023-5 PubMed GONUTS page

[PMID:17057717-15] Sivanathan, V et al. (2006) The FtsK gamma domain directs oriented DNA translocation by interacting with KOPS. Nat. Struct. Mol. Biol. 13 965-72 PubMed GONUTS page

[PMID:21371996-16] Grainge, I et al. (2011) Activation of XerCD-dif recombination by the FtsK DNA translocase. Nucleic Acids Res. 39 5140-8 PubMed GONUTS page

[PMID:24302254-17] Bisicchia, P et al. (2013) The N-terminal membrane-spanning domain of the Escherichia coli DNA translocase FtsK hexamerizes at midcell. MBio 4 e00800-13 PubMed GONUTS page

[PMID:19246541-18] Bonné, L et al. (2009) Asymmetric DNA requirements in Xer recombination activation by FtsK. Nucleic Acids Res. 37 2371-80 PubMed GONUTS page

[PMID:16301526-19] Levy, O et al. (2005) Identification of oligonucleotide sequences that direct the movement of the Escherichia coli FtsK translocase. Proc. Natl. Acad. Sci. U.S.A. 102 17618-23 PubMed GONUTS page

[PMID:15919996-20] Daley, DO et al. (2005) Global topology analysis of the Escherichia coli inner membrane proteome. Science 308 1321-3 PubMed GONUTS page

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ECOLI:FTSK

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