Difference between revisions of "FtsZ"
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= This gene is a member of the following [[regulons]] = | = This gene is a member of the following [[regulons]] = | ||
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{{SubtiWiki regulon|[[SigH regulon]]}}, | {{SubtiWiki regulon|[[SigH regulon]]}}, | ||
{{SubtiWiki regulon|[[WalR regulon]]}} | {{SubtiWiki regulon|[[WalR regulon]]}} | ||
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* '''[[Sigma factor]]:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/sites/entrez/1569582 PubMed], [[SigH]] [http://www.ncbi.nlm.nih.gov/sites/entrez/1569582 PubMed] | * '''[[Sigma factor]]:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/sites/entrez/1569582 PubMed], [[SigH]] [http://www.ncbi.nlm.nih.gov/sites/entrez/1569582 PubMed] | ||
− | * '''Regulation:''' activated by [[WalR]] [http://www.ncbi.nlm.nih.gov/sites/entrez/10878122 | + | * '''Regulation:''' |
− | + | ** activated by [[WalR]] [http://www.ncbi.nlm.nih.gov/sites/entrez/10878122 PubMed] | |
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
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* '''Additional information:''' | * '''Additional information:''' |
Revision as of 13:19, 14 July 2011
- Description: cell-division initiation protein (septum formation)
Gene name | ftsZ |
Synonyms | ts-1 |
Essential | yes PubMed |
Product | cell-division initiation protein (septum formation) |
Function | formation of Z-ring |
MW, pI | 40 kDa, 4.814 |
Gene length, protein length | 1146 bp, 382 aa |
Immediate neighbours | ftsA, bpr |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
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: BSU15290
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: ftsZ family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- UniProt: P17865
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody: available in the Jeff Errington lab
Labs working on this gene/protein
- Imrich Barak, Slovak Academy of Science, Bratislava, Slovakia homepage
- Leendert Hamoen, CBCB, Newcastle University, UK
Your additional remarks
References
Reviews
Matthew T Cabeen, Christine Jacobs-Wagner
The bacterial cytoskeleton.
Annu Rev Genet: 2010, 44;365-92
[PubMed:21047262]
[WorldCat.org]
[DOI]
(I p)
Marc Bramkamp, Suey van Baarle
Division site selection in rod-shaped bacteria.
Curr Opin Microbiol: 2009, 12(6);683-8
[PubMed:19884039]
[WorldCat.org]
[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]
[WorldCat.org]
[DOI]
(I p)
Peter L Graumann
Cytoskeletal elements in bacteria.
Annu Rev Microbiol: 2007, 61;589-618
[PubMed:17506674]
[WorldCat.org]
[DOI]
(P p)
Linda A Amos, Fusinita van den Ent, Jan Löwe
Structural/functional homology between the bacterial and eukaryotic cytoskeletons.
Curr Opin Cell Biol: 2004, 16(1);24-31
[PubMed:15037301]
[WorldCat.org]
[DOI]
(P p)
Additional reviews: PubMed
FtsZ as antibacterial drug target
Other original Publications
Additional publications: PubMed