SpoIVFB

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  • Description: intramembrane metalloprotease, processing of pro-sigma-K to active SigK

Gene name spoIVFB
Synonyms
Essential no
Product intramembrane metalloprotease
Function processing of pro-sigma-K to active SigK
Gene expression levels in SubtiExpress: spoIVFB
Interactions involving this protein in SubtInteract: SpoIVFB
MW, pI 33 kDa, 8.483
Gene length, protein length 864 bp, 288 aa
Immediate neighbours rplU, spoIVFA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
SpoIVFB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SpoIVFB expression.png















Categories containing this gene/protein

sigma factors and their control, proteolysis, sporulation proteins, membrane proteins

This gene is a member of the following regulons

SigE regulon

The gene

Basic information

  • Locus tag: BSU27970

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: processing of pro-sigma-K to active SigK PubMed
  • Protein family: peptidase M50B family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
    • C-terminal cystathionine-beta-synthase (CBS) domain, this domain binds ATP PubMed
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity: ATP regulates substrate access to the active site and renders cleavage sensitive to the cellular energy level PubMed

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • 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

Reviews

Additional reviews: PubMed

Gu Chen, Xu Zhang
New insights into S2P signaling cascades: regulation, variation, and conservation.
Protein Sci: 2010, 19(11);2015-30
[PubMed:20836086] [WorldCat.org] [DOI] (I p)

Original Publications