SubtiBank SubtiBank
ftsZ
An ordered knock out library of all non-essential genes in B. subtilis is now available at Addgene. Information on ordering a copy can be found here. See Koo et al. 2017 for details about library construction.

ftsZ

cell-division initiation protein (septum formation)
locus
BSU15290
pI
4.81
mw
40.20 kDa
protein length
382 aa Sequence Blast
gene length
1146 bp Sequence Blast
function
formation of Z-ring
product
cell-division initiation protein (septum formation)
essential
yes
synonyms
ts-1

Genomic Context

      

categories

  • [category|SW 1|Cellular processes] → [category|SW 1.1|Cell envelope and cell division] → [category|SW 1.1.8|Cell division] → [category|SW 1.1.8.2|Other genes]
  • [category|SW 6|Groups of genes] → [category|SW 6.1|Essential genes]
  • [category|SW 6|Groups of genes] → [category|SW 6.2|Membrane proteins]
  • Gene

    Coordinates
    1,597,832 → 1,598,980

    Phenotypes of a mutant

  • essential [Pubmed|12682299], but dispensible in [protein|search|L-forms] [Pubmed|25358088]
  • The protein

    Protein family

  • ftsZ family (according to Swiss-Prot)
  • Effectors of protein activity

  • Z ring formation is inhibited upon binding of [protein|08EBBA57B807F8C27C37BEB275DF5E206935C698|MciZ] to FtsZ
  • bundling of FtsZ protofilaments into strikingly long and regular tubular structures reminiscent of eukaryotic microtubules requires the prior formation of large ring polymers of [protein|DB09F1C36257F511A84A083967A25A9D46744D14|SepF] [Pubmed|21224850]
  • interaction with [protein|7A606B8E952AE8CA4F9A62008BA4B156725BB5B5|UgtP] inhibits [protein|41872E2EF00C79918DD077F2EF78F37E24FEB110|FtsZ] filament formation [Pubmed|22931116]
  • FtsZ polymerization is inhibited by interaction with [protein|8C94C9598A823A8405B3E1FA0124E21D90845B8E|MinC] [Pubmed|23577149]
  • Z ring formation requires [protein|953DE0F0B81894ECFF4C0693511AC238BF3D0C0A|PdhA] in a pyruvate-dependent manner [Pubmed|24825009]
  • Structure

  • [PDB|2VAM]
  • [PDB|2RHL] (dimer with GDP)
  • [PDB|4U39] ([protein|41872E2EF00C79918DD077F2EF78F37E24FEB110|FtsZ]-[protein|search|F150B9B75C8352950B9BB71E29CB156B66AA6CDD] complex) [Pubmed|25848052]
  • [SW|Localization]

  • septal at the cell membrane [Pubmed|20566861]
  • septal localization partially depends on the proton motive force [Pubmed|20566861]
  • [protein|559DEDC9887B811EF80994526256ADC48BA51CE3|Noc] and the Min system ensure the efficient utilization of the division site at midcell in by ensuring [protein|41872E2EF00C79918DD077F2EF78F37E24FEB110|Z ring]]] placement [Pubmed|22457634]
  • [protein|41872E2EF00C79918DD077F2EF78F37E24FEB110|FtsZ] is anchored to the cell membrane by either [protein|672EA84D7725BE21F649DF30A11EB4E0EDFC3925|FtsA] or [protein|DB09F1C36257F511A84A083967A25A9D46744D14|SepF] [Pubmed|24218584,16159787]
  • Additional information

  • the novel antibiotic ADEP (acyldepsipeptides) causes [protein|41872E2EF00C79918DD077F2EF78F37E24FEB110|FtsZ] degradation via dysregulation [protein|CB06A70DE7462CEB7AF5D8C28943C878DD56DE1A|ClpP] activity (activity occurs even in the absence of an ATPase subunit ([protein|86A2F2F65290F4471D6FD03B694821C66C180D8A|ClpC], [protein|8C5B14FE5E03427F9A598C75D4081FA0D6696299|ClpE], or [protein|297F53DAD3351E0C55108DD2C93B78FFB174438C|ClpX])) [Pubmed|21969594]
  • Expression and Regulation

    Operons

    genes
    [gene|672EA84D7725BE21F649DF30A11EB4E0EDFC3925|ftsA]-[gene|41872E2EF00C79918DD077F2EF78F37E24FEB110|ftsZ]
    description
    [Pubmed|1569582]

    sigma factors

  • [protein|360F48D576DE950DF79C1A2677B7A35A8D8CC30C|SigA]: sigma factor, [Pubmed|1569582], in [regulon|360F48D576DE950DF79C1A2677B7A35A8D8CC30C|SigA regulon]
  • [protein|DC3449D5F195E5C2E9E14FEC95396C8F1FDF73B4|SigH]: sigma factor, [Pubmed|1569582], in [regulon|DC3449D5F195E5C2E9E14FEC95396C8F1FDF73B4|SigH regulon]
  • regulatory mechanism

  • [protein|7F340423A34CE40D1F1AA8D373F7C4B859A6496D|WalR]: activation, in [regulon|7F340423A34CE40D1F1AA8D373F7C4B859A6496D|WalR regulon]
  • regulation

  • activated by [protein|search|WalR] [Pubmed|10878122]
  • additional information

  • half-life of the ''[SW|ftsZ]'' mRNA: 2.2 min [Pubmed|26110430]
  • view in new tab

    Biological materials

    Expression vector

  • GP2009: expression of ''ftsZ''-Strep under control of the ''ftsZ'' promoter (based on [SW|pGP1389]), available in [SW|Jörg Stülke]'s lab
  • two-hybrid system

  • ''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([SW|BACTH]), available in [SW|Jörg Stülke]'s lab
  • Antibody

  • available in the [SW|Jeff Errington] lab
  • Labs working on this gene/protein

  • [SW|Imrich Barak], Slovak Academy of Science, Bratislava, Slovakia [http://imb.savba.sk/~barak/ homepage]
  • [SW|Leendert Hamoen], CBCB, Newcastle University, UK
  • References

    Reviews

  • 22047950,22575476,21119015,19680248,19884039,17506674,15037301,21047262,21981908,24550892,25957405,26706151,27620716,28254403,28500523,28697666,28975672
  • FtsZ as antibacterial drug target

  • 19583568,20410587,16174771,20212044,20615583,21276094,23841620,23855511,24079270,24749867,25062781,25972861,26258635,28082038,28168121
  • Other original Publications

  • 24007276,15288790,15317782,12180929,9364910,10323866,19212404,15942012,12007411,16420366,25176632,16159787,10747015,16950129,16796675,10322023,9495766,9287012,1569582,10878122,17718511,11395470,10449747,17662947,12368265,18284588,8600030,18588879,7592498,19136590,19429628,19141479,19843223,16484179,20199598,20566861,20711458,20807205,20933427,15948963,12700262,22298780,22457634,22730127,22984350,23577149,22931116,22912848,21224850,23692518,23701187,23836667,16159787,24300445,24316672,24825009,18573169,25403286,25358088,25848052,26247422,23098212,23237472,26601800,26360512,27410746,27629358,27752253,28465423,28616148