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sepF [2017-8-11 16:0:3]
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sepF [2017-8-11 16:0:3]

part of the divisome, recruits FtsZ to the membrane
locus
BSU15390
pI
4.86
mw
17.01 kDa
protein length
149 aa Sequence Blast
gene length
447 bp Sequence Blast
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]

    • Gene

    Coordinates
    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 ''[gene|DB09F1C36257F511A84A083967A25A9D46744D14|sepF]'' mutation in combination with a constitutively active form of [protein|7F340423A34CE40D1F1AA8D373F7C4B859A6496D|WalR] ([protein|7F340423A34CE40D1F1AA8D373F7C4B859A6496D|WalR]-R204C) results in the formation of cell wall-less L-forms [Pubmed|22122227]
  • the ''sepF'' mutation is synthetically lethal in combination with an ''[gene|B317D7E51824DD70EF84E4D5D7290D601BF4FAB6|ezrA]'' mutation or an ''[gene|672EA84D7725BE21F649DF30A11EB4E0EDFC3925|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|41872E2EF00C79918DD077F2EF78F37E24FEB110|FtsZ] protofilaments into strikingly long and regular tubular structures reminiscent of eukaryotic microtubules [Pubmed|21224850]
  • SepF anchors [protein|41872E2EF00C79918DD077F2EF78F37E24FEB110|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|41872E2EF00C79918DD077F2EF78F37E24FEB110|FtsZ]-binding domain [Pubmed|24218584]

    • Structure

  • [PDB|3ZIH] (the [protein|41872E2EF00C79918DD077F2EF78F37E24FEB110|FtsZ]-binding C-terminal domain) [Pubmed|24218584]

    • [SW|Localization]

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

    • Expression and Regulation

    Operons

    genes
    [gene|ECCE99438DBFC52DA7236CB4F6486DD004CADF73|ylmD]-[gene|31789A170CB624BF8210C915F40007F802F5C81B|ylmE]-[gene|DB09F1C36257F511A84A083967A25A9D46744D14|sepF]-[gene|2B2D285D5A8F160808A21DCF07BDB924365970C5|ylmG]-[gene|BD5ACF930DD63E258D71569326752C9A1D7B9324|ylmH]
    description
    [Pubmed|16420366]

    regulatory mechanism

  • [protein|2C54FE2ADC82FF414D732018C90649D477A925AD|Spo0A]: repression, [Pubmed|14651647], in [regulon|2C54FE2ADC82FF414D732018C90649D477A925AD|Spo0A regulon]

    • regulation

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

    Mutant

  • MGNA-B172 (ylmF::erm), available at the [https://shigen.nig.ac.jp/bsub/resource/strainGeneDisrupted/detail/1171 NBRP B. subtilis, Japan]
  • GP2008 (''[gene|DB09F1C36257F511A84A083967A25A9D46744D14|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