ftsK:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

Standard name

FtsK

Synonyms

DNA-binding membrane protein required for chromosome resolution and partitioning[1], B0890[2][1], DinH[2][1], FtsK[2][1] , dinH, ECK0881, JW0873, b0890

Product description

essential cell division protein FtsK [3][2][4];

Component of Xer site-specific recombination system[4][5]

DNA translocase at septal ring sorting daughter chromsomes[6][5]

Couples cell division and chromosome segregation. [7]

Required at an early step in septation. [3]

EC number (for enzymes)


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Notes

Function

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<protect> Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0051301

cell division

PMID:9721304[8]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0007059

chromosome segregation

PMID:12034757[5]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0051301

cell division

PMID:7592387[9]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0000166

nucleotide binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002543

F

Seeded from EcoCyc (v14.0)

complete

GO:0007059

chromosome segregation

PMID:17805344[10]

IMP: Inferred from Mutant Phenotype

P

expression of the cytoplasmic domain of FtsK facilitates chromosome segregation in parC(ts) and parE(ts) cells

complete

GO:0000166

nucleotide binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0547

F

Seeded from EcoCyc (v14.0)

complete

GO:0005886

plasma membrane

PMID:10922461[11]

EXP: Inferred from Experiment

C

complete

GO:0005524

ATP binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002543

F

Seeded from EcoCyc (v14.0)

complete

GO:0051301

cell division

PMID:9294448[12]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0005524

ATP binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0067

F

Seeded from EcoCyc (v14.0)

complete

GO:0006970

response to osmotic stress

PMID:9294448[12]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0005887

integral to plasma membrane

PMID:10922461[11]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc (v14.0)

complete

GO:0003677

DNA binding

PMID:18722176[13]

IDA: Inferred from Direct Assay

F

complete

GO:0007049

cell cycle

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002543

P

Seeded from EcoCyc (v14.0)

complete

GO:0016887

ATPase activity

PMID:18722176[13]

IDA: Inferred from Direct Assay

F

complete

GO:0007049

cell cycle

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0131

P

Seeded from EcoCyc (v14.0)

complete

GO:0007059

chromosome segregation

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002543

P

Seeded from EcoCyc (v14.0)

complete

GO:0007059

chromosome segregation

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0159

P

Seeded from EcoCyc (v14.0)

complete

GO:0007059

chromosome segregation

PMID:12034757[5]

IGI: Inferred from Genetic Interaction

P

Seeded from EcoCyc (v14.0)

Missing: with/from

GO:0007059

chromosome segregation

PMID:12034757[5]

IGI: Inferred from Genetic Interaction

UniProtKB:P0A734 UniProtKB:P0AEZ3 UniProtKB:P18196


P

Seeded from EcoCyc (v14.0)

complete

GO:0015616

DNA translocase activity

PMID:16301526[14]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc (v14.0)

complete

GO:0043565

sequence-specific DNA binding

PMID:17041598[15]

IMP: Inferred from Mutant Phenotype

F

Seeded from EcoCyc (v14.0)

complete

GO:0043565

sequence-specific DNA binding

PMID:17057717[16]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc (v14.0)

complete

GO:0045941

positive regulation of transcription

PMID:9294448[12]

IMP: Inferred from Mutant Phenotype

P

Seeded from EcoCyc (v14.0)

complete

GO:0016020

membrane

PMID:9723913[3]

IDA: Inferred from Direct Assay

C

complete

GO:0016020

membrane

PMID:10922461[11]

IDA: Inferred from Direct Assay

C

complete

GO:0071236

cellular response to antibiotic

PMID:9723913[3]

IMP: Inferred from Mutant Phenotype

P

mitomycin C

complete

GO:0007059

chromosome segregation

PMID:9829960[17]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0015616

DNA translocase activity

PMID:19854947[18]

IDA: Inferred from Direct Assay

F

complete

GO:0016887

ATPase activity

PMID:19854947[18]

IDA: Inferred from Direct Assay

F

complete

GO:0007059

chromosome segregation

PMID:19854947[18]

IDA: Inferred from Direct Assay

P

complete

GO:0051301

cell division

PMID:9829960[17]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0007059

chromosome segregation

PMID:19854947[18]

IPI: Inferred from Physical Interaction

UniProtKB:P0A8P6 UniProtKB:P0A8P8


P

complete

GO:0045893

positive regulation of transcription, DNA-dependent

PMID:9294448[12]

IMP: Inferred from Mutant Phenotype

P

increases PuspA activity in stationary phase

complete

Contributes to

GO:0006265

DNA topological change

PMID:20081205[19]

IDA: Inferred from Direct Assay

P

stimulates Topo IV's ability to relax positively supercoiled DNA

complete

GO:0009651

response to salt stress

PMID:9294448[12]

IMP: Inferred from Mutant Phenotype

P

complete

Contributes to

GO:0007059

chromosome segregation

PMID:20081205[19]

IDA: Inferred from Direct Assay

P

stimulates Topo IV's decatenation ability

complete

GO:0000920

cytokinetic cell separation

PMID:9294448[12]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0007059

chromosome segregation

PMID:12034757[5]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0007059

chromosome segregation

PMID:12034757[5]

IGI: Inferred from Genetic Interaction

UniProtKB:P0A734 UniProtKB:P0AEZ3 UniProtKB:P18196


P

complete

Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner Type Partner Notes References Evidence

Protein

Subunits of Xer site-specific recombination system

could be indirect

Protein

aceE

PMID:15690043[20]

Experiment(s):EBI-888719

Protein

rpsJ

PMID:19402753[21]

LCMS(ID Probability):99.6

Protein

yfiD

PMID:19402753[21]

LCMS(ID Probability):99.6

Protein

ParC subunit of Topo IV

PMID:12939258[22]

Protein

Either subunit of the XerCD Recombinase

PMID:19854947[18]

Triplex Displacement Assays

Protein

FtsZ and FtsA

FtsK localization depends on FtsZ and FtsA prior localization

PMID:9723913[3]


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Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

Compartment Description Evidence Reference/Source Notes

plasma membrane

C-terminus localized in the cytoplasm with 6 predicted transmembrane domains

Daley et al. (2005) [23]

Inner membrane

GFP fusion localization

PMID:9495771[24]

Signal sequence in the N-terminal domain of the protein

Inner membrane

PhoA and beta-gal assays

PMID:10922461[11]

Cytosol

FtsK (818-1329)

Microscopy

PMID:11114887[25]


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Notes

Structure and Physical Properties

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<protect> Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Name
Sequence

at EcoCyc

MSQEYIEDKE VTLTKLSSGR RLLEALLILI VLFAVWLMAA LLSFNPSDPS WSQTAWHEPI
HNLGGMPGAW LADTLFFIFG VMAYTIPVII VGGCWFAWRH QSSDEYIDYF AVSLRIIGVL
ALILTSCGLA AINADDIWYF ASGGVIGSLL STTLQPLLHS SGGTIALLCV WAAGLTLFTG
WSWVTIAEKL GGWILNILTF ASNRTRRDDT WVDEDEYEDD EEYEDENHGK QHESRRARIL
RGALARRKRL AEKFINPMGR QTDAALFSGK RMDDDEEITY TARGVAADPD DVLFSGNRAT
QPEYDEYDPL LNGAPITEPV AVAAAATTAT QSWAAPVEPV TQTPPVASVD VPPAQPTVAW
QPVPGPQTGE PVIAPAPEGY PQQSQYAQPA VQYNEPLQQP VQPQQPYYAP AAEQPAQQPY
YAPAPEQPVA GNAWQAEEQQ STFAPQSTYQ TEQTYQQPAA QEPLYQQPQP VEQQPVVEPE
PVVEETKPAR PPLYYFEEVE EKRAREREQL AAWYQPIPEP VKEPEPIKSS LKAPSVAAVP
PVEAAAAVSP LASGVKKATL ATGAAATVAA PVFSLANSGG PRPQVKEGIG PQLPRPKRIR
VPTRRELASY GIKLPSQRAA EEKAREAQRN QYDSGDQYND DEIDAMQQDE LARQFAQTQQ
QRYGEQYQHD VPVNAEDADA AAEAELARQF AQTQQQRYSG EQPAGANPFS LDDFEFSPMK
ALLDDGPHEP LFTPIVEPVQ QPQQPVAPQQ QYQQPQQPVP PQPQYQQPQQ PVAPQPQYQQ
PQQPVAPQQQ YQQPQQPVAP QQQYQQPQQP VAPQPQDTLL HPLLMRNGDS RPLHKPTTPL
PSLDLLTPPP SEVEPVDTFA LEQMARLVEA RLADFRIKAD VVNYSPGPVI TRFELNLAPG
VKAARISNLS RDLARSLSTV AVRVVEVIPG KPYVGLELPN KKRQTVYLRE VLDNAKFRDN
PSPLTVVLGK DIAGEPVVAD LAKMPHLLVA GTTGSGKSVG VNAMILSMLY KAQPEDVRFI
MIDPKMLELS VYEGIPHLLT EVVTDMKDAA NALRWCVNEM ERRYKLMSAL GVRNLAGYNE
KIAEADRMMR PIPDPYWKPG DSMDAQHPVL KKEPYIVVLV DEFADLMMTV GKKVEELIAR
LAQKARAAGI HLVLATQRPS VDVITGLIKA NIPTRIAFTV SSKIDSRTIL DQAGAESLLG
MGDMLYSGPN STLPVRVHGA FVRDQEVHAV VQDWKARGRP QYVDGITSDS ESEGGAGGFD
GAEELDPLFD QAVQFVTEKR KASISGVQRQ FRIGYNRAAR IIEQMEAQGI VSEQGHNGNR
EVLAPPPFD
Length

1,329

Mol. Wt

146.661 kDa

pI

4.8 (calculated)

Extinction coefficient

173,040 - 173,540 (calc based on 46 Y, 19 W, and 4 C residues)


Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

Type Residues Description Notes References

Domain

947..1161

PF01580 FtsK/SpoIIIE family

PMID:19920124[26]

Domain

1261..1327

PF09397 Ftsk gamma domain

PMID:19920124[26]

<motif_map/>

tmhmm.php?gene=ftsK&show=pic&.jpg
Click the image to view raw output from TMHMM.

Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures

<beststructure> gene=ftsK taxon=562,83333 </beststructure>

Models

View models at:

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Structure figures

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Notes

  • Membrane topology studies using phoA and lacZ fusions are described in Dorazi et al.(2000)[11]
  • Crystal structure of P. aeruginosa FtsK complexed with KOPS with a putative molecular mechanism for loading and translocation may be found in Lowe et al. (2008)[13].
  • FtsK links chromosome segregation to septation via its domain structure. The N-terminal domain is required for septation and its C-terminal domain is required for chromosome segregation[27].

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference

Antibody

raised against FtsK(447-729)

isolated from rabbit [3]

Purification protocol

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Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

NCBI (Protein) (EcoliWiki Page)

GI:16128857

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:945102

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0003027

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P46889

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:G6464

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG13226

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:945102

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120003064

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB3016

Escherichia coli str. K-12 substr. MG1655

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Notes

Links

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References

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

  1. 1.0 1.1 1.2 1.3 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. 2.0 2.1 2.2 2.3 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. 3.0 3.1 3.2 3.3 3.4 3.5 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
  4. 4.0 4.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  5. 5.0 5.1 5.2 5.3 5.4 5.5 5.6 Capiaux, H et al. (2002) A dual role for the FtsK protein in Escherichia coli chromosome segregation. EMBO Rep. 3 532-6 PubMed
  6. EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  7. Robertson, S (1992) Putting pen to paper. Aust Crit Care 5 2 PubMed
  8. Draper, GC et al. (1998) Only the N-terminal domain of FtsK functions in cell division. J. Bacteriol. 180 4621-7 PubMed
  9. Begg, KJ et al. (1995) A new Escherichia coli cell division gene, ftsK. J. Bacteriol. 177 6211-22 PubMed
  10. Grainge, I et al. (2007) Unlinking chromosome catenanes in vivo by site-specific recombination. EMBO J. 26 4228-38 PubMed
  11. 11.0 11.1 11.2 11.3 11.4 Dorazi, R & Dewar, SJ (2000) Membrane topology of the N-terminus of the Escherichia coli FtsK division protein. FEBS Lett. 478 13-8 PubMed
  12. 12.0 12.1 12.2 12.3 12.4 12.5 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
  13. 13.0 13.1 13.2 13.3 Löwe, J et al. (2008) Molecular mechanism of sequence-directed DNA loading and translocation by FtsK. Mol. Cell 31 498-509 PubMed
  14. 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
  15. Ptacin, JL et al. (2006) Identification of the FtsK sequence-recognition domain. Nat. Struct. Mol. Biol. 13 1023-5 PubMed
  16. 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
  17. 17.0 17.1 Yu, XC et al. (1998) Role of the C terminus of FtsK in Escherichia coli chromosome segregation. J. Bacteriol. 180 6424-8 PubMed
  18. 18.0 18.1 18.2 18.3 18.4 Graham, JE et al. (2010) FtsK translocation on DNA stops at XerCD-dif. Nucleic Acids Res. 38 72-81 PubMed
  19. 19.0 19.1 19.2 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
  20. Butland, G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433 531-7 PubMed
  21. 21.0 21.1 Hu, P et al. (2009) Global functional atlas of Escherichia coli encompassing previously uncharacterized proteins. PLoS Biol. 7 e96 PubMed
  22. 22.0 22.1 Espeli, O et al. (2003) A physical and functional interaction between Escherichia coli FtsK and topoisomerase IV. J. Biol. Chem. 278 44639-44 PubMed
  23. Daley, DO et al. (2005) Global topology analysis of the Escherichia coli inner membrane proteome. Science 308 1321-3 PubMed
  24. Yu, XC et al. (1998) Localization of cell division protein FtsK to the Escherichia coli septum and identification of a potential N-terminal targeting domain. J. Bacteriol. 180 1296-304 PubMed
  25. Barre, FX et al. (2000) FtsK functions in the processing of a Holliday junction intermediate during bacterial chromosome segregation. Genes Dev. 14 2976-88 PubMed
  26. 26.0 26.1 Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed
  27. Bigot, S et al. (2007) FtsK, a literate chromosome segregation machine. Mol. Microbiol. 64 1434-41 PubMed
  28. Aussel, L et al. (2002) FtsK Is a DNA motor protein that activates chromosome dimer resolution by switching the catalytic state of the XerC and XerD recombinases. Cell 108 195-205 PubMed

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