Letunic et al. (2017) Nucleic Acids Res doi: 10.1093/nar/gkx922
Letunic et al. (2020) Nucleic Acids Res doi: 10.1093/nar/gkaa937

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Ftsk_gamma

SMART accession number:	SM00843
Description:	This domain directs oriented DNA translocation and forms a winged helix structure. Mutated proteins with substitutions in the FtsK gamma DNA-recognition helix are impaired in DNA binding.
Interpro abstract (IPR018541):	This domain directs oriented DNA translocation and forms a winged helix structure [ (PUBMED:17057717) ]. Mutated proteins with substitutions in the FtsK gamma DNA-recognition helix are impaired in DNA binding [ (PUBMED:17057717) ].
Family alignment:	View or CHROMA formatHMM/Web logoCLUSTALW formatMSF formatFASTA formatPIR format

There are 25892 Ftsk_gamma domains in 25774 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Taxonomic distribution of proteins containing Ftsk_gamma domain.

  This tree includes only several representative species. The complete taxonomic breakdown of all proteins with Ftsk_gamma domain is also avaliable.

  Click on the protein counts, or double click on taxonomic names to display all proteins containing Ftsk_gamma domain in the selected taxonomic class.

• Cellular role (predicted cellular role)

• Cellular role: chromatin
  

• Literature (relevant references for this domain)

• Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

  • Sivanathan V et al.
  • The FtsK gamma domain directs oriented DNA translocation by interactingwith KOPS.
  • Nat Struct Mol Biol. 2006; 13: 965-72
  • Display abstract

  • The bacterial septum-located DNA translocase FtsK coordinates circularchromosome segregation with cell division. Rapid translocation of DNA byFtsK is directed by 8-base-pair DNA motifs (KOPS), so that newlyreplicated termini are brought together at the developing septum, therebyfacilitating completion of chromosome segregation. Translocase functionsreside in three domains, alpha, beta and gamma. FtsKalphabeta arenecessary and sufficient for ATP hydrolysis-dependent DNA translocation,which is modulated by FtsKgamma through its interaction with KOPS. Bysolving the FtsKgamma structure by NMR, we show that gamma is awinged-helix domain. NMR chemical shift mapping localizes the DNA-bindingsite on the gamma domain. Mutated proteins with substitutions in theFtsKgamma DNA-recognition helix are impaired in DNA binding and KOPSrecognition, yet remain competent in DNA translocation and XerCD-difsite-specific recombination, which facilitates the late stages ofchromosome segregation.

• Structure (3D structures containing this domain)

• 3D Structures of Ftsk_gamma domains in PDB

  PDB code	Main view	Title
  2ius		E. coli FtsK motor domain
  2iut		P. aeruginosa FtsK motor domain, dimeric
  2j5o		Pseudomonas aeruginosa FtsK gamma domain
  2j5p		E. coli FtsK gamma domain
  2ve8		Xray structure of FtsK gamma domain (P. aeruginosa)
  2ve9		Xray structure of KOPS bound gamma domain of FtsK (P. aeruginosa)
  5dcf		5DCF

• Links (links to other resources describing this domain)

• INTERPRO	IPR018541
  PFAM	Ftsk_gamma

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