Difference between revisions of "FtsL"
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* '''Effectors of protein activity:''' degraded by [[RasP]], stabilized against [[RasP]] cleavage by [[DivIC]] {{PubMed|20644139}} | * '''Effectors of protein activity:''' degraded by [[RasP]], stabilized against [[RasP]] cleavage by [[DivIC]] {{PubMed|20644139}} | ||
| − | * '''Interactions:''' [[RasP]]-[[FtsL]], [[DivIC]]-[[FtsL]] {{PubMed|10844672}} | + | * '''Interactions:''' |
| + | ** [[RasP]]-[[FtsL]], [[DivIC]]-[[FtsL]] {{PubMed|10844672}} | ||
| + | ** [[PbpB]]-[[DivIB]]-([[FtsL]]-[[DivIC]])2 {{PubMed|20870765}}, as part of the [[divisome]] | ||
* '''Localization:''' cell membrane (according to Swiss-Prot) | * '''Localization:''' cell membrane (according to Swiss-Prot) | ||
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<pubmed> 20836086 </pubmed> | <pubmed> 20836086 </pubmed> | ||
==Original Publications== | ==Original Publications== | ||
| − | <pubmed>9720875,10792716,16936019,16549676,17020588,8636036,10986263, 11994149, 10844672,19429628 20644139 </pubmed> | + | <pubmed>9720875,10792716,16936019,16549676,17020588,8636036,10986263, 11994149, 10844672,19429628 20644139 20870765</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 16:41, 28 September 2010
- 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
| |
Contents
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):
- Localization: cell membrane (according to Swiss-Prot)
Database entries
- Structure:
- UniProt: Q07867
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews=
Original Publications
Susan L Rowland, Kimberly D Wadsworth, Scott A Robson, Carine Robichon, Jon Beckwith, Glenn F King
Evidence from artificial septal targeting and site-directed mutagenesis that residues in the extracytoplasmic β domain of DivIB mediate its interaction with the divisomal transpeptidase PBP 2B.
J Bacteriol: 2010, 192(23);6116-25
[PubMed:20870765]
[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)
