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][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 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|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 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 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, UKReferences
Reviews
22047950,22575476,21119015,19680248,19884039,17506674,15037301,21047262,21981908,24550892,25957405,26706151 FtsZ as antibacterial drug target
19583568,20410587,16174771,20212044,20615583,21276094,23841620,23855511,24079270,24749867,25062781,25972861,26258635 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 
