FtsL

• Description: cell-division protein (septum formation), controls together with EzrA dynamics of the FtsZ ring
  
  

Gene name	ftsL
Synonyms	ylxB, yllD
Essential	yes PubMed
Product	cell-division protein
Function	septum formation
MW, pI	12 kDa, 10.083
Gene length, protein length	351 bp, 117 aa
Immediate neighbours	mraW, pbpB
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU15150

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: ftsL family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity: degraded by RasP

• Interactions: RasP-FtsL, DivIC-FtsL

• Localization: cell membrane (according to Swiss-Prot)

Database entries

• Structure:

• Swiss prot entry: Q07867

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon:

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information: FtsL is degraded by RasP

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Pamela Gamba, Jan-Willem Veening, Nigel J Saunders, Leendert W Hamoen, Richard A Daniel
Two-step assembly dynamics of the Bacillus subtilis divisome.
J Bacteriol: 2009, 191(13);4186-94
[PubMed:19429628] [WorldCat.org] [DOI] (I p)

Scott A Robson, Katharine A Michie, Joel P Mackay, Elizabeth Harry, Glenn F King
The Bacillus subtilis cell division proteins FtsL and DivIC are intrinsically unstable and do not interact with one another in the absence of other septasomal components.
Mol Microbiol: 2002, 44(3);663-74
[PubMed:11994149] [WorldCat.org] [DOI] (P p)

J Sievers, J Errington
The Bacillus subtilis cell division protein FtsL localizes to sites of septation and interacts with DivIC.
Mol Microbiol: 2000, 36(4);846-55
[PubMed:10844672] [WorldCat.org] [DOI] (P p)