FlgN
- Description: flagellar filament assembly protein
Gene name | yvyG |
Synonyms | yviC |
Essential | no |
Product | flagellar filament assembly protein |
Function | flagellar filament assembly |
Gene expression levels in SubtiExpress: flgN | |
Interactions involving this protein in SubtInteract: FlgN | |
MW, pI | 18 kDa, 8.81 |
Gene length, protein length | 480 bp, 160 aa |
Immediate neighbours | flgK, flgM |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
motility and chemotaxis, phosphoproteins
This gene is a member of the following regulons
ComK regulon, DegU regulon, SigD regulon
The gene
Basic information
- Locus tag: BSU35420
Phenotypes of a mutant
- non-motile cells PubMed
Database entries
- BsubCyc: BSU35420
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- essential for flagellar filament assembly PubMed
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Effectors of protein activity:
Database entries
- BsubCyc: BSU35420
- Structure:
- UniProt: P39808
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Lynne S Cairns, Victoria L Marlow, Taryn B Kiley, Christopher Birchall, Adam Ostrowski, Phillip D Aldridge, Nicola R Stanley-Wall
FlgN is required for flagellum-based motility by Bacillus subtilis.
J Bacteriol: 2014, 196(12);2216-26
[PubMed:24706744]
[WorldCat.org]
[DOI]
(I p)
Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742]
[WorldCat.org]
[DOI]
(I p)
Yi-Huang Hsueh, Loralyn M Cozy, Lok-To Sham, Rebecca A Calvo, Alina D Gutu, Malcolm E Winkler, Daniel B Kearns
DegU-phosphate activates expression of the anti-sigma factor FlgM in Bacillus subtilis.
Mol Microbiol: 2011, 81(4);1092-108
[PubMed:21736639]
[WorldCat.org]
[DOI]
(I p)
Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307]
[WorldCat.org]
[DOI]
(P p)
Mark J Pallen, Charles W Penn, Roy R Chaudhuri
Bacterial flagellar diversity in the post-genomic era.
Trends Microbiol: 2005, 13(4);143-9
[PubMed:15817382]
[WorldCat.org]
[DOI]
(P p)
D B Mirel, P Lauer, M J Chamberlin
Identification of flagellar synthesis regulatory and structural genes in a sigma D-dependent operon of Bacillus subtilis.
J Bacteriol: 1994, 176(15);4492-500
[PubMed:8045879]
[WorldCat.org]
[DOI]
(P p)
J A Londoño-Vallejo, D Dubnau
comF, a Bacillus subtilis late competence locus, encodes a protein similar to ATP-dependent RNA/DNA helicases.
Mol Microbiol: 1993, 9(1);119-31
[PubMed:8412657]
[WorldCat.org]
[DOI]
(P p)