Difference between revisions of "FtsL"

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=References=
 
=References=
=Reviews==
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==Reviews==
 
<pubmed> 20836086 </pubmed>
 
<pubmed> 20836086 </pubmed>
 
==Original Publications==
 
==Original Publications==
<pubmed>9720875,10792716,16936019,16549676,17020588,8636036,10986263, 11994149, 10844672,19429628 20644139 20870765 21219466</pubmed>
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'''Additional references:''' {{PubMed|20870765}}
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<pubmed>9720875,10792716,16936019,16549676,17020588,8636036,10986263, 11994149, 10844672,19429628 20644139 21219466</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 10:21, 12 January 2011

  • 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
FtsL context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

cell division, essential genes, membrane proteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU15150

Phenotypes of a mutant

essential PubMed

Database entries

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

Additional information

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, stabilized against RasP cleavage by DivIC PubMed
  • Localization: cell membrane (according to Swiss-Prot)

Database entries

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

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information: FtsL is degraded by RasP PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Gu Chen, Xu Zhang
New insights into S2P signaling cascades: regulation, variation, and conservation.
Protein Sci: 2010, 19(11);2015-30
[PubMed:20836086] [WorldCat.org] [DOI] (I p)

Original Publications

Additional references: PubMed

Tatsuya Fukushima, Isako Furihata, Robyn Emmins, Richard A Daniel, James A Hoch, Hendrik Szurmant
A role for the essential YycG sensor histidine kinase in sensing cell division.
Mol Microbiol: 2011, 79(2);503-22
[PubMed:21219466] [WorldCat.org] [DOI] (I p)

Inga Wadenpohl, Marc Bramkamp
DivIC stabilizes FtsL against RasP cleavage.
J Bacteriol: 2010, 192(19);5260-3
[PubMed:20644139] [WorldCat.org] [DOI] (I p)

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)

Marc Bramkamp, Louise Weston, Richard A Daniel, Jeff Errington
Regulated intramembrane proteolysis of FtsL protein and the control of cell division in Bacillus subtilis.
Mol Microbiol: 2006, 62(2);580-91
[PubMed:17020588] [WorldCat.org] [DOI] (P p)

Richard A Daniel, Marie-Françoise Noirot-Gros, Philippe Noirot, Jeff Errington
Multiple interactions between the transmembrane division proteins of Bacillus subtilis and the role of FtsL instability in divisome assembly.
J Bacteriol: 2006, 188(21);7396-404
[PubMed:16936019] [WorldCat.org] [DOI] (P p)

Yoshikazu Kawai, Naotake Ogasawara
Bacillus subtilis EzrA and FtsL synergistically regulate FtsZ ring dynamics during cell division.
Microbiology (Reading): 2006, 152(Pt 4);1129-1141
[PubMed:16549676] [WorldCat.org] [DOI] (P 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
Analysis of the essential cell division gene ftsL of Bacillus subtilis by mutagenesis and heterologous complementation.
J Bacteriol: 2000, 182(19);5572-9
[PubMed:10986263] [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)

R A Daniel, J Errington
Intrinsic instability of the essential cell division protein FtsL of Bacillus subtilis and a role for DivIB protein in FtsL turnover.
Mol Microbiol: 2000, 36(2);278-89
[PubMed:10792716] [WorldCat.org] [DOI] (P p)

R A Daniel, E J Harry, V L Katis, R G Wake, J Errington
Characterization of the essential cell division gene ftsL(yIID) of Bacillus subtilis and its role in the assembly of the division apparatus.
Mol Microbiol: 1998, 29(2);593-604
[PubMed:9720875] [WorldCat.org] [DOI] (P p)

R A Daniel, A M Williams, J Errington
A complex four-gene operon containing essential cell division gene pbpB in Bacillus subtilis.
J Bacteriol: 1996, 178(8);2343-50
[PubMed:8636036] [WorldCat.org] [DOI] (P p)