FtsA
- Description: cell-division protein, membrane anchor for FtsZ
Gene name | ftsA |
Synonyms | spoIIN |
Essential | yes PubMed |
Product | cell-division protein |
Function | formation of Z-ring |
Interactions involving this protein in SubtInteract: FtsA | |
MW, pI | 47 kDa, 5.094 |
Gene length, protein length | 1320 bp, 440 aa |
Immediate neighbours | sbp, ftsZ |
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: BSU15280
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: ftsA/mreB family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: P28264
- 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:
Labs working on this gene/protein
Your additional remarks
References
Reviews
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)
Original Publications
Henrik Strahl, Leendert W Hamoen
Membrane potential is important for bacterial cell division.
Proc Natl Acad Sci U S A: 2010, 107(27);12281-6
[PubMed:20566861]
[WorldCat.org]
[DOI]
(I p)
José Roberto Tavares, Robson F de Souza, Guilherme Louzada Silva Meira, Frederico J Gueiros-Filho
Cytological characterization of YpsB, a novel component of the Bacillus subtilis divisome.
J Bacteriol: 2008, 190(21);7096-107
[PubMed:18776011]
[WorldCat.org]
[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]
[WorldCat.org]
[DOI]
(P p)
S O Jensen, L S Thompson, E J Harry
Cell division in Bacillus subtilis: FtsZ and FtsA association is Z-ring independent, and FtsA is required for efficient midcell Z-Ring assembly.
J Bacteriol: 2005, 187(18);6536-44
[PubMed:16159787]
[WorldCat.org]
[DOI]
(P p)
Jennifer T Kemp, Adam Driks, Richard Losick
FtsA mutants of Bacillus subtilis impaired in sporulation.
J Bacteriol: 2002, 184(14);3856-63
[PubMed:12081956]
[WorldCat.org]
[DOI]
(P p)
A Feucht, I Lucet, M D Yudkin, J Errington
Cytological and biochemical characterization of the FtsA cell division protein of Bacillus subtilis.
Mol Microbiol: 2001, 40(1);115-25
[PubMed:11298280]
[WorldCat.org]
[DOI]
(P p)
Keisuke Fukuchi, Yasuhiro Kasahara, Kei Asai, Kazuo Kobayashi, Shigeki Moriya, Naotake Ogasawara
The essential two-component regulatory system encoded by yycF and yycG modulates expression of the ftsAZ operon in Bacillus subtilis.
Microbiology (Reading): 2000, 146 ( Pt 7);1573-1583
[PubMed:10878122]
[WorldCat.org]
[DOI]
(P p)
X Wang, J Huang, A Mukherjee, C Cao, J Lutkenhaus
Analysis of the interaction of FtsZ with itself, GTP, and FtsA.
J Bacteriol: 1997, 179(17);5551-9
[PubMed:9287012]
[WorldCat.org]
[DOI]
(P p)
M A Strauch
Delineation of AbrB-binding sites on the Bacillus subtilis spo0H, kinB, ftsAZ, and pbpE promoters and use of a derived homology to identify a previously unsuspected binding site in the bsuB1 methylase promote.
J Bacteriol: 1995, 177(23);6999-7002
[PubMed:7592498]
[WorldCat.org]
[DOI]
(P p)
G Gonzy-Tréboul, C Karmazyn-Campelli, P Stragier
Developmental regulation of transcription of the Bacillus subtilis ftsAZ operon.
J Mol Biol: 1992, 224(4);967-79
[PubMed:1569582]
[WorldCat.org]
[DOI]
(P p)