cell-division initiation protein (septum formation)
function
formation of Z-ring
product
cell-division initiation protein (septum formation)
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 FtsZbundling 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 tabBiological materials
Expression vectors
GP2009: expression of ''ftsZ''-Strep under control of the ''ftsZ'' promoter (based on [SW|pGP1389]), available in [SW|Jörg Stülke]'s labtwo-hybrid system
''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([SW|BACTH]), available in [SW|Jörg Stülke]'s labAntibody
available in the [SW|Jeff Errington] lablabs
[SW|Imrich Barak], Slovak Academy of Science, Bratislava, Slovakia [http://imb.savba.sk/~barak/ homepage][SW|Leendert Hamoen], CBCB, Newcastle University, UKReferences
Reviews
22047950,22575476,21119015,19680248,19884039,17506674,15037301,21047262,21981908,24550892,25957405,26706151,27620716,28254403,28500523,28697666,28975672,29355854 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