ftsZ

ftsZ
168

cell-division initiation protein (septum formation)

locus
BSU_15290
Molecular weight
40.20 kDa
pI
4.81
Protein length
382 aaSequenceBlast
Gene length
1149 bpSequenceBlast
function
formation of Z-ring
product
cell-division initiation protein (septum formation), member of the [wiki|divisome]
essential
yes
synonyms
ftsZ, ts-1
Outlinks
BsubCyc SubtiList UniProt STRING Genoscapist PaperBLAST

Genomic Context

Categories containing this gene/protein

List of homologs in different organisms, belongs to COG0206 (Galperin et al., 2021)

This gene is a member of the following regulons

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 (single member, according to UniProt)
Structure
[PDB|2VAM]
[PDB|2RHL] (dimer  with GDP)
[PDB|4U39] ([protein|41872E2EF00C79918DD077F2EF78F37E24FEB110|ftsZ]-[protein|08EBBA57B807F8C27C37BEB275DF5E206935C698|mciZ] complex) [Pubmed|25848052]
[AF|P17865]
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]
[wiki|Localization]
during vegetative growth: uniform [protein|672EA84D7725BE21F649DF30A11EB4E0EDFC3925|ftsA]-[protein|41872E2EF00C79918DD077F2EF78F37E24FEB110|ftsZ] rings around the leading edge of the invaginating medial septum to orchestrate [wiki|cell division] ([protein|672EA84D7725BE21F649DF30A11EB4E0EDFC3925|ftsA] is proximal to the membrane and tethers [protein|41872E2EF00C79918DD077F2EF78F37E24FEB110|ftsZ]) [pubmed|34018921]
at the onset of sporulation: [protein|672EA84D7725BE21F649DF30A11EB4E0EDFC3925|ftsA]-[protein|41872E2EF00C79918DD077F2EF78F37E24FEB110|ftsZ] filaments are assembled only on the mother cell side of the invaginating polar septum, this depends on [protein|7C8DFE00A2B2B30CC8BEB35055D92CC2E4128F3A|spoIIE] [pubmed|34018921]
Expression and Regulation
Operons
genes
[gene|672EA84D7725BE21F649DF30A11EB4E0EDFC3925|ftsA]-[gene|41872E2EF00C79918DD077F2EF78F37E24FEB110|ftsZ]
description
[Pubmed|1569582]
regulation
activated by [protein|search|WalR] [Pubmed|10878122]
regulatory mechanism
[protein|7F340423A34CE40D1F1AA8D373F7C4B859A6496D|walR]: activation, in [regulon|protein:7F340423A34CE40D1F1AA8D373F7C4B859A6496D|walR regulon]
sigma factors
[protein|360F48D576DE950DF79C1A2677B7A35A8D8CC30C|sigA]: sigma factor, [Pubmed|1569582], in [regulon|protein:360F48D576DE950DF79C1A2677B7A35A8D8CC30C|sigA regulon]
[protein|DC3449D5F195E5C2E9E14FEC95396C8F1FDF73B4|sigH]: sigma factor, [Pubmed|1569582], in [regulon|protein:DC3449D5F195E5C2E9E14FEC95396C8F1FDF73B4|sigH regulon]
additional information
half-life of the ''[wiki|ftsZ]'' mRNA: 2.2 min [Pubmed|26110430]
Open in new tab

[gene|672EA84D7725BE21F649DF30A11EB4E0EDFC3925|ftsA]→[gene|41872E2EF00C79918DD077F2EF78F37E24FEB110|ftsZ]

2024-11-21 09:53:44

ghost

115

68a077d38d141bb7e809cea3546c5dc557d7fb61

A67267E496C6E05B8143FD5F6AD1E46A65A9877D

Biological materials
Expression vectors
GP2009: expression of ''ftsZ''-Strep under control of the ''ftsZ'' promoter (based on [wiki|pGP1389]), available in [wiki|Jörg Stülke]'s lab
two-hybrid system
''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([wiki|BACTH]), available in [wiki|Jörg Stülke]'s lab
Antibody
available in the [wiki|Jeff Errington] lab
labs
[wiki|Imrich Barak], Slovak Academy of Science, Bratislava, Slovakia [http://imb.savba.sk/~barak/ homepage]
[wiki|Leendert Hamoen], CBCB, Newcastle University, UK
References
Reviews
22047950,22575476,21119015,19680248,19884039,17506674,15037301,21047262,21981908,24550892,25957405,26706151,27620716,28254403,28500523,28697666,28975672,29355854,30855188,35081523,35638784,36411352,36695643,38821027
Original Publications
24007276,15288790,15317782,12180929,9364910,10323866,19212404,15942012,12007411,16420366,25176632,16159787,10747015,16950129,16796675,10322023,9495766,9287012,1569582,10878122,17718511,11395470,10449747,17662947,12368265,18284588,8600030,18588879,7592498,19136590,19429628,19141479,19843223,16484179,20199598,20566861,20711458,20807205,20933427,15948963,12700262,22298780,22457634,22730127,22984350,23577149,22931116,22912848,21224850,23692518,23701187,23836667,16159787,24300445,24316672,24825009,18573169,25403286,25358088,25848052,26247422,23098212,23237472,26601800,26360512,27410746,27629358,27752253,28465423,28616148,30636070,32184253,32198113,32605984,33077634,33649500,33737746,33907196,34018921,34521822,35495694,35799411,36215496,36515540,37790399,38198550,38480901,38502707,38992051,39416851
FtsZ as antibacterial drug target
19583568,20410587,16174771,20212044,20615583,21276094,23841620,23855511,24079270,24749867,25062781,25972861,26258635,28082038,28168121,31249557,36009372

41872E2EF00C79918DD077F2EF78F37E24FEB110

Page visits: 13070

Time of last update: 2024-11-29 19:00:51

Author of last update: Jstuelk