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sepF [Tue Dec 13 2016 11:16:33 GMT+0100 (CET)]
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sepF [Tue Dec 13 2016 11:16:33 GMT+0100 (CET)]

part of the divisome, recruits FtsZ to the membrane
locus
BSU15390
pI
4.00
mw
17.00 kDa
function
recruitment of FtsZ
product
FtsZ-interacting protein
essential
no
synonyms
ylmF
Outlinks
KEGGBsubCycSubtiListUniProtExpression Browser

Genomic Context

      

categories

  • [category|SW 1|Cellular processes] → [category|SW 1.1|Cell envelope and cell division] → [category|SW 1.1.8|Cell division] → [category|SW 1.1.8.2|Other genes]
  • [category|SW 6|Groups of genes] → [category|SW 6.2|Membrane proteins]

    • [SW|Categories] containing this gene/protein

  • [SW|cell division], [SW|membrane proteins]

    • This gene is a member of the following [SW|regulons]

  • [SW|Spo0A regulon]

    • Gene

    Coordinates on the chromosome (coding sequence)
    1,610,865 -> 1,611,314

    Phenotypes of a mutant

  • perturbation of the formation of properly formed division septa
  • less efficient cell division results in longer cells. Electron microscopy reveals strongly distorted division septa.
  • the ''[protein|search|sepF]'' mutation in combination with a constitutively active form of [protein|search|WalR] ([protein|search|WalR]-R204C) results in the formation of cell wall-less L-forms [Pubmed|22122227]
  • the ''sepF'' mutation is synthetically lethal in combination with an ''[protein|search|ezrA]'' mutation or an ''[protein|search|ftsA]'' mutation [Pubmed|24218584]

    • The protein

    Catalyzed reaction/ biological activity

  • SepF assembles into very large (∼50 nm diameter) rings. These rings are able to bundle [protein|search|FtsZ] protofilaments into strikingly long and regular tubular structures reminiscent of eukaryotic microtubules [Pubmed|21224850]
  • SepF anchors [protein|search|FtsZ] bundles to the membrane [Pubmed|24218584]

    • Protein family

  • sepF family (according to Swiss-Prot)

    • [SW|Domains]

  • N-terminal amphipatic helix for membrane binding [Pubmed|24218584]
  • C-terminal globular [protein|search|FtsZ]-binding domain [Pubmed|24218584]

    • Structure

  • [PDB|3ZIH] (the [protein|search|FtsZ]-binding C-terminal domain) [Pubmed|24218584]

    • [SW|Localization]

  • septum [Pubmed|16420366]
  • membrane [Pubmed|24218584]

    • [SW|Interactions]

  • forms filaments that are made up of dimers [Pubmed|24218584]
  • [protein|search|FtsZ] (extreme C terminus of [protein|search|FtsZ])-[protein|search|SepF] [Pubmed|24218584,22912848,16420366]

    • Expression and Regulation

    Operon

  • ''[protein|search|ylmD]-[protein|search|ylmE]-[protein|search|sepF]-[protein|search|ylmG]-[protein|search|ylmH]'' [Pubmed|16420366]

    • Regulation

  • repressed under conditions that trigger sporulation ([SW|Spo0A]) [Pubmed|14651647]

    • Regulatory mechanism

  • [SW|Spo0A]: transcription repression [Pubmed|14651647]

    • Biological materials

    Mutant

  • GP2008 (''[protein|search|sepF]''::''spc''), available in [SW|Jörg Stülke]'s lab

    • Labs working on this gene/protein

  • [SW|Leendert Hamoen], CBCB, Newcastle University, UK
  • [SW|Shu Ishikawa], Nara Institute of Science and Technology, Nara, Japan

    • References

    Reviews

  • 19680248,22126136

    • Original Publications

  • 16420366,16796675,14651647,24218584,22912848,21224850,22122227