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ftsZ [Sun Jan 15 2017 12:21:11 GMT+0100 (CET)]
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ftsZ [Sun Jan 15 2017 12:21:11 GMT+0100 (CET)]

cell-division initiation protein (septum formation)
locus
BSU15290
pI
4.00
mw
40.00 kDa
function
formation of Z-ring
product
cell-division initiation protein (septum formation)
essential
yes
synonyms
ts-1
Outlinks
KEGGBsubCycSubtiListUniProtExpression Browser

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]

    • [SW|Categories] containing this gene/protein

  • [SW|cell division], [SW|essential genes], [SW|membrane proteins]

    • This gene is a member of the following [SW|regulons]

  • [SW|SigH regulon], [SW|WalR regulon]

    • Gene

    Coordinates on the chromosome (coding sequence)
    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|search|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|search|SepF] [Pubmed|21224850]
  • interaction with [protein|search|UgtP] inhibits [protein|search|FtsZ] filament formation [Pubmed|22931116]
  • FtsZ polymerization is inhibited by interaction with [protein|search|MinC] [Pubmed|23577149]
  • Z ring formation requires [protein|search|PdhA] in a pyruvate-dependent manner [Pubmed|24825009]

    • Structure

  • [PDB|2VAM]
  • [PDB|2RHL] (dimer with GDP)
  • [PDB|4U39] ([protein|search|FtsZ]-[protein|search|MciZ] complex) [Pubmed|25848052]

    • [SW|Localization]

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

    • [SW|Interactions]

  • [protein|search|FtsZ]-[protein|search|ZapA] [Pubmed|19843223]
  • [protein|search|FtsZ]-[protein|search|EzrA] [Pubmed|25403286,10449747]
  • [protein|search|FtsZ]-[SW|SpoIIE]
  • [protein|search|FtsZ]-[protein|search|FtsA] [Pubmed|16159787]
  • [protein|search|FtsZ]-[protein|search|FtsZ] [Pubmed|17662947]
  • [protein|search|MciZ]-[protein|search|FtsZ] [Pubmed|18284588], KD: 150 nM [Pubmed|25848052]
  • [protein|search|FtsZ] (extreme C terminus of [protein|search|FtsZ])-[protein|search|SepF] [Pubmed|24218584,22912848,16420366]
  • [protein|search|RefZ]-[protein|search|FtsZ] [Pubmed|22730127]
  • [protein|search|FtsZ]-[protein|search|LytE] [Pubmed|16950129]
  • [protein|search|UgtP]-[protein|search|FtsZ], this interaction inhibits [protein|search|FtsZ] filament formation [Pubmed|22931116]
  • [protein|search|FtsZ] (C-terminal domain)-[protein|search|MinC] [Pubmed|23577149]
  • [protein|search|WalK]-[protein|search|FtsZ] [Pubmed|18573169]

    • Additional information

  • the novel antibiotic ADEP (acyldepsipeptides) causes [protein|search|FtsZ] degradation via dysregulation [protein|search|ClpP] activity (activity occurs even in the absence of an ATPase subunit ([protein|search|ClpC], [protein|search|ClpE], or [protein|search|ClpX])) [Pubmed|21969594]

    • Expression and Regulation

    Operon

  • ''[protein|search|ftsA]-[protein|search|ftsZ]'' [Pubmed|1569582]

    • [SW|Sigma factor]

  • [protein|search|SigA] [Pubmed|1569582], [protein|search|SigH] [Pubmed|1569582]

    • Regulation

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

    • Additional information

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

    • 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

    • FtsZ as antibacterial drug target

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

    • 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