Difference between revisions of "FtsA"

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(Extended information on the protein)
Line 8: Line 8:
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''spoIIN ''
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''spoIIN ''
|style="background:#ABCDEF;" align="center"| '''Essential''' || yes [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed]
|style="background:#ABCDEF;" align="center"| '''Essential''' || no
|style="background:#ABCDEF;" align="center"| '''Product''' || cell-division protein
|style="background:#ABCDEF;" align="center"| '''Product''' || cell-division protein
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= [[Categories]] containing this gene/protein =
= [[Categories]] containing this gene/protein =
{{SubtiWiki category|[[cell division]]}},
{{SubtiWiki category|[[cell division]]}},
{{SubtiWiki category|[[essential genes]]}},
{{SubtiWiki category|[[membrane proteins]]}}
{{SubtiWiki category|[[membrane proteins]]}}
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===Phenotypes of a mutant ===
===Phenotypes of a mutant ===
* cells become elongated {{PubMed|24218584}}
essential [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed]
=== Database entries ===
=== Database entries ===
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=== Additional information===
=== Additional information===
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* '''Kinetic information:'''
* '''Kinetic information:'''
* '''Domains:'''  
* '''[[Domains]]:'''  
* '''Modification:'''
* '''Modification:'''
* '''Cofactor(s):'''
* '''Cofactors:'''
* '''Effectors of protein activity:'''
* '''Effectors of protein activity:'''
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<pubmed> 19680248 </pubmed>
<pubmed> 19680248 </pubmed>
==Original Publications==
==Original Publications==
<pubmed>16796675,12081956,16159787,11298280,18776011,9287012,1569582,10878122,7592498, 20566861 23036588 23701187 </pubmed>
<pubmed>16796675,12081956,16159787,11298280,18776011,9287012,1569582,10878122,7592498, 20566861 23036588 23701187 24218584</pubmed>
[[Category:Protein-coding genes]]
[[Category:Protein-coding genes]]

Revision as of 10:23, 15 December 2013

  • Description: cell-division protein, membrane anchor for FtsZ

Gene name ftsA
Synonyms spoIIN
Essential no
Product cell-division protein
Function formation of Z-ring
Gene expression levels in SubtiExpress: ftsA
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
Sequences Protein DNA DNA_with_flanks
Genetic context
FtsA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
FtsA expression.png

Categories containing this gene/protein

cell division, membrane proteins

This gene is a member of the following regulons

SigH regulon, WalR regulon

The gene

Basic information

  • Locus tag: BSU15280

Phenotypes of a mutant

  • cells become elongated 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:
  • Modification:
  • Cofactors:
  • Effectors of protein activity:

Database entries

  • Structure:
  • 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



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

Ramona Duman, Shu Ishikawa, Ilkay Celik, Henrik Strahl, Naotake Ogasawara, Paulina Troc, Jan Löwe, Leendert W Hamoen
Structural and genetic analyses reveal the protein SepF as a new membrane anchor for the Z ring.
Proc Natl Acad Sci U S A: 2013, 110(48);E4601-10
[PubMed:24218584] [WorldCat.org] [DOI] (I p)

Erik Nico Trip, Jan-Willem Veening, Eric J Stewart, Jeff Errington, Dirk-Jan Scheffers
Balanced transcription of cell division genes in Bacillus subtilis as revealed by single cell analysis.
Environ Microbiol: 2013, 15(12);3196-209
[PubMed:23701187] [WorldCat.org] [DOI] (I p)

Parminder Singh, Ravindra D Makde, Saikat Ghosh, Jayant Asthana, Vinay Kumar, Dulal Panda
Assembly of Bacillus subtilis FtsA: effects of pH, ionic strength and nucleotides on FtsA assembly.
Int J Biol Macromol: 2013, 52;170-6
[PubMed:23036588] [WorldCat.org] [DOI] (I p)

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)