From SubtiWiki
(Redirected from YlmF)
Jump to: navigation, search
  • Description: part of the divisome, recruits FtsZ to the membrane

Gene name sepF
Synonyms ylmF
Essential no
Product FtsZ-interacting protein
Function recruitment of FtsZ
Gene expression levels in SubtiExpress: sepF
Interactions involving this protein in SubtInteract: SepF
MW, pI 17 kDa, 4.863
Gene length, protein length 447 bp, 149 aa
Immediate neighbours ylmE, ylmG
Sequences Protein DNA DNA_with_flanks
Genetic context
YlmF context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SepF expression.png

Categories containing this gene/protein

cell division, membrane proteins

This gene is a member of the following regulons

Spo0A regulon

The gene

Basic information

  • Locus tag: BSU15390

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 sepF mutation in combination with a constitutively active form of WalR (WalR-R204C) results in the formation of cell wall-less L-forms PubMed
  • the sepF mutation is synthetically lethal in combination with an ezrA mutation or an ftsA mutation PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • SepF assembles into very large (∼50 nm diameter) rings. These rings are able to bundle FtsZ protofilaments into strikingly long and regular tubular structures reminiscent of eukaryotic microtubules PubMed
    • SepF anchors FtsZ bundles to the membrane PubMed
  • Protein family: sepF family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • repressed under conditions that trigger sporulation (Spo0A) PubMed
  • Regulatory mechanism:
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 437 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 837 PubMed

Biological materials

  • Mutant:
    • YK204 (sepF::spc), available in the labs of Leendert Hamoen and Jörg Stülke
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Leendert Hamoen, CBCB, Newcastle University, UK

Shu Ishikawa, Nara Institute of Science and Technology, Nara, Japan

Your additional remarks

SepF mutation is synthetic lethal in combination with an ezrA mutation or an ftsA mutation.



Kevin M Devine
Bacterial L-forms on tap: an improved methodology to generate Bacillus subtilis L-forms heralds a new era of research.
Mol Microbiol: 2012, 83(1);10-3
[PubMed:22126136] [] [DOI] (I p)

David W Adams, Jeff Errington
Bacterial cell division: assembly, maintenance and disassembly of the Z ring.
Nat Rev Microbiol: 2009, 7(9);642-53
[PubMed:19680248] [] [DOI] (I p)

Original Publications

Ramona Duman, Shu Ishikawa, Ilkay Celik, Henrik Strahl, Naotake Ogasawara, Paulina Troc, Jan Löwe, Leendert W Hamoen
Structural and genetic analyses reveal the protein SepF as a new membrane anchor for the Z ring.
Proc Natl Acad Sci U S A: 2013, 110(48);E4601-10
[PubMed:24218584] [] [DOI] (I p)

Ewa Król, Sebastiaan P van Kessel, Laura S van Bezouwen, Neeraj Kumar, Egbert J Boekema, Dirk-Jan Scheffers
Bacillus subtilis SepF binds to the C-terminus of FtsZ.
PLoS One: 2012, 7(8);e43293
[PubMed:22912848] [] [DOI] (I p)

Patricia Domínguez-Cuevas, Romain Mercier, Mark Leaver, Yoshikazu Kawai, Jeff Errington
The rod to L-form transition of Bacillus subtilis is limited by a requirement for the protoplast to escape from the cell wall sacculus.
Mol Microbiol: 2012, 83(1);52-66
[PubMed:22122227] [] [DOI] (I p)

Muhammet E Gündoğdu, Yoshikazu Kawai, Nada Pavlendova, Naotake Ogasawara, Jeff Errington, Dirk-Jan Scheffers, Leendert W Hamoen
Large ring polymers align FtsZ polymers for normal septum formation.
EMBO J: 2011, 30(3);617-26
[PubMed:21224850] [] [DOI] (I p)

Shu Ishikawa, Yoshikazu Kawai, Konosuke Hiramatsu, Masayoshi Kuwano, Naotake Ogasawara
A new FtsZ-interacting protein, YlmF, complements the activity of FtsA during progression of cell division in Bacillus subtilis.
Mol Microbiol: 2006, 60(6);1364-80
[PubMed:16796675] [] [DOI] (P p)

Leendert W Hamoen, Jean-Christophe Meile, Wouter de Jong, Philippe Noirot, Jeff Errington
SepF, a novel FtsZ-interacting protein required for a late step in cell division.
Mol Microbiol: 2006, 59(3);989-99
[PubMed:16420366] [] [DOI] (P p)

Virginie Molle, Masaya Fujita, Shane T Jensen, Patrick Eichenberger, José E González-Pastor, Jun S Liu, Richard Losick
The Spo0A regulon of Bacillus subtilis.
Mol Microbiol: 2003, 50(5);1683-701
[PubMed:14651647] [] [DOI] (P p)