Difference between revisions of "SpoIVFB"

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(Reviews)
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* '''[[Localization]]:'''  
 
* '''[[Localization]]:'''  
 
** integral membrane protein {{PubMed|11959848}}
 
** integral membrane protein {{PubMed|11959848}}
** outermost membrane surrounding the forespore {{PubMed|9078383}}
+
** mother cell membrane {{PubMed|24243021}}
  
 
=== Database entries ===
 
=== Database entries ===
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==Original Publications==
 
==Original Publications==
<pubmed>11959848,9501233,12940997,1577688,12060714,9078383,1942049,10611287,15383836 16818230 19805276 15699190 23585539 23995631 15087499</pubmed>
+
<pubmed>11959848,9501233,12940997,1577688,12060714,9078383,1942049,10611287,15383836 16818230 19805276 15699190 23585539 23995631 15087499 24243021 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 10:02, 3 December 2013

  • 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
Sequences Protein DNA DNA_with_flanks
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

Lee Kroos, Yoshinori Akiyama
Biochemical and structural insights into intramembrane metalloprotease mechanisms.
Biochim Biophys Acta: 2013, 1828(12);2873-85
[PubMed:24099006] [WorldCat.org] [DOI] (P p)

Noël Molière, Kürşad Turgay
General and regulatory proteolysis in Bacillus subtilis.
Subcell Biochem: 2013, 66;73-103
[PubMed:23479438] [WorldCat.org] [DOI] (P p)

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)

Michael S Wolfe
Intramembrane-cleaving proteases.
J Biol Chem: 2009, 284(21);13969-73
[PubMed:19189971] [WorldCat.org] [DOI] (P p)


Original Publications