sepF
168
part of the [wiki|divisome], recruits [protein|41872E2EF00C79918DD077F2EF78F37E24FEB110|ftsZ] to the membrane and [protein|DF77B46666595E86081C5345C91E08F86DF9FAEE|sftA] to the Z-ring, determines the thickness of the septal cell wall
locus
BSU_15390
Molecular weight
17.01 kDa
pI
4.86
function
recruitment of [protein|41872E2EF00C79918DD077F2EF78F37E24FEB110|ftsZ], recruits [protein|DF77B46666595E86081C5345C91E08F86DF9FAEE|sftA] to the Z-ring
product
[protein|41872E2EF00C79918DD077F2EF78F37E24FEB110|ftsZ]-interacting protein, member of the [wiki|divisome]
essential
no
synonyms
sepF, ylmF
Outlinks
Genomic Context
Categories containing this gene/protein
List of homologs in different organisms, belongs to COG1799 (Galperin et al., 2021)
This gene is a member of the following regulons
Gene
Coordinates
1,610,865 → 1,611,314
Phenotypes of a mutant
perturbation of the formation of properly formed division septa
less efficient cell division results in longer cells. Electron microscopy reveals strongly distorted division septa.
the [gene|DB09F1C36257F511A84A083967A25A9D46744D14|sepF] mutation in combination with a constitutively active form of [protein|7F340423A34CE40D1F1AA8D373F7C4B859A6496D|walR] ([protein|7F340423A34CE40D1F1AA8D373F7C4B859A6496D|walR]-R204C) results in the formation of cell wall-less L-forms [Pubmed|22122227]
the [gene|DB09F1C36257F511A84A083967A25A9D46744D14|sepF] mutation is synthetically lethal in combination with an [gene|B317D7E51824DD70EF84E4D5D7290D601BF4FAB6|ezrA] mutation or an [gene|672EA84D7725BE21F649DF30A11EB4E0EDFC3925|ftsA] mutation [Pubmed|24218584]
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The protein
Catalyzed reaction/ biological activity
SepF assembles into very large (∼50 nm diameter) rings. These rings are able to bundle [protein|41872E2EF00C79918DD077F2EF78F37E24FEB110|ftsZ] protofilaments into strikingly long and regular tubular structures reminiscent of eukaryotic microtubules [Pubmed|21224850]
SepF anchors [protein|41872E2EF00C79918DD077F2EF78F37E24FEB110|ftsZ] bundles to the membrane [Pubmed|24218584]
Protein family
sepF family (single member, according to UniProt)
[wiki|Domains]
N-terminal amphipatic helix for membrane binding [Pubmed|24218584]
C-terminal globular [protein|41872E2EF00C79918DD077F2EF78F37E24FEB110|ftsZ]-binding domain [Pubmed|24218584]
Structure
[PDB|3ZIH] (the [protein|41872E2EF00C79918DD077F2EF78F37E24FEB110|ftsZ]-binding C-terminal domain) [Pubmed|24218584]
[AF|O31728]
[wiki|Localization]
septum [Pubmed|16420366]
membrane [Pubmed|24218584]
colocalizes with the Z-ring [pubmed|38198550]
Expression and Regulation
Operons
genes
[gene|ECCE99438DBFC52DA7236CB4F6486DD004CADF73|ylmD]-[gene|31789A170CB624BF8210C915F40007F802F5C81B|ylmE]-[gene|DB09F1C36257F511A84A083967A25A9D46744D14|sepF]-[gene|2B2D285D5A8F160808A21DCF07BDB924365970C5|ylmG]-[gene|BD5ACF930DD63E258D71569326752C9A1D7B9324|ylmH]
description
[Pubmed|16420366]
regulation
repressed under conditions that trigger sporulation ([wiki|Spo0A]) [Pubmed|14651647]
regulatory mechanism
[protein|2C54FE2ADC82FF414D732018C90649D477A925AD|spo0A]: repression, [Pubmed|14651647], in [regulon|protein:2C54FE2ADC82FF414D732018C90649D477A925AD|spo0A regulon]
Biological materials
Mutant
MGNA-B172 (ylmF::erm), available at the [https://shigen.nig.ac.jp/bsub/resource/strainGeneDisrupted/detail/1171 NBRP B. subtilis, Japan]
GP2008 ([gene|DB09F1C36257F511A84A083967A25A9D46744D14|sepF]::''spc''), available in [wiki|Jörg Stülke]'s lab
BKE15390 (Δ[gene|DB09F1C36257F511A84A083967A25A9D46744D14|sepF]::erm trpC2) available at [http://bgsc.org/getdetail.php?bgscid=BKE15390 BGSC], [Pubmed|28189581], upstream reverse: _UP1_CATACTCATTGCTGTACACC, downstream forward: _UP4_GAACATCAGAGGTGGTAAAG
BKK15390 (Δ[gene|DB09F1C36257F511A84A083967A25A9D46744D14|sepF]::kan trpC2) available at [http://bgsc.org/getdetail.php?bgscid=BKK15390 BGSC], [Pubmed|28189581], upstream reverse: _UP1_CATACTCATTGCTGTACACC, downstream forward: _UP4_GAACATCAGAGGTGGTAAAG
labs
[wiki|Leendert Hamoen], CBCB, Newcastle University, UK
[wiki|Shu Ishikawa], Nara Institute of Science and Technology, Nara, Japan
References
Reviews
Original Publications
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Time of last update: 2024-04-19 06:20:35
Author of last update: Jstuelk