Hag

• Description: flagellin protein, about 20,000 subunits make up one flagellum
  
  

Gene name	hag
Synonyms
Essential	no
Product	flagellin protein
Function	motility and chemotaxis
Gene expression levels in SubtiExpress: hag
Interactions involving this protein in SubtInteract: Hag
Metabolic function and regulation of this protein in SubtiPathways: Hag
MW, pI	32 kDa, 4.782
Gene length, protein length	912 bp, 304 aa
Immediate neighbours	yvyC, csrA
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

motility and chemotaxis, most abundant proteins

This gene is a member of the following regulons

CodY regulon, CsrA regulon, ScoC regulon, SigD regulon

The gene

Basic information

• Locus tag: BSU35360

Phenotypes of a mutant

• no swarming motility on B medium. PubMed
• not essential for pellicle biofilm formation, but mutant is outcompeted by the wild-type strain when competed during pellicle formation PubMed
• few hours delay in pellicle development PubMed
• mutant has increased fitness in planktonic culture when competed with the wild-type NCIB3610 strain PubMed

Database entries

• BsubCyc: BSU35360

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: bacterial flagellin family (according to Swiss-Prot)

• Paralogous protein(s): YvzB (C-terminal domain of Hag)

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactors:

• Effectors of protein activity:

• Interactions:
  • FlhA-Hag PubMed
  • FlhA-(FliS-Hag) PubMed
  • FliS-Hag PubMed
  • FliW-Hag PubMed

• Localization:
  • extracellular (no signal peptide), major component of the secretome PubMed
  • membrane PubMed

Database entries

• BsubCyc: BSU35360

• Structure: 3A5X (from Salmonella typhimurium, 42% identity)

• UniProt: P02968

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: hag PubMed

• Expression browser: hag PubMed

• Sigma factor: SigD PubMed

• Regulation:
  • repressed during growth in the presence of branched chain amino acids (CodY) PubMed

• Regulatory mechanism:
  • CodY: transcription repression PubMed
  • CsrA: translation inhibition PubMed
  • ScoC: transcription repression PubMed

• Additional information:
  • the hag gene is strongly overexpressed in a ymdB mutant (loss of bistable gene expression) PubMed
  • belongs to the 100 most abundant proteins PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 150241 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 280953 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 9552 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 11147 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 24114 PubMed

Biological materials

• Mutant: GP901 (aphA3), GP902 (tet) PubMed, both available in Jörg Stülke's lab
  • 1A915 ( hag::cat), PubMed, available at BGSC
  • 1A783 ( hag::erm), PubMed, available at BGSC
  • 1A842 ( hag::kan), PubMed, available at BGSC
  • DS1677 (marker-less in NCIB3610) PubMed
  • TB191 amyE::Phy-sfgfp (marker-less in NCIB3610 with constitutive expressed sfgfp) PubMed
  • TB207 amyE::Phy-mKATE2 (marker-less in NCIB3610 with constitutive expressed mKATE2) PubMed

• Expression vector:
  • expression in B. subtilis, in pBQ200: pGP1089, available in Jörg Stülke's lab

• lacZ fusion: pGP1035 (in pAC6), pGP755 (in pAC7), there is also a series of promoter deletion variants in pAC6 and pAC7 PubMed, all available in Jörg Stülke's lab

• GFP fusion: BP494 (bglS:: (hag-promoter-cfp-aphA3)), BP496 (amyE:: (hag-promoter-iyfp-cat)), available in Jörg Stülke's lab

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

• Daniel Kearns

References

Reviews

Sampriti Mukherjee, Daniel B Kearns
The structure and regulation of flagella in Bacillus subtilis.
Annu Rev Genet: 2014, 48;319-40
[PubMed:25251856] [WorldCat.org] [DOI] (I p)

Tony Romeo, Christopher A Vakulskas, Paul Babitzke
Post-transcriptional regulation on a global scale: form and function of Csr/Rsm systems.
Environ Microbiol: 2013, 15(2);313-24
[PubMed:22672726] [WorldCat.org] [DOI] (I p)