Difference between revisions of "SpoIVFB"

From SubtiWiki
Jump to: navigation, search
Line 29: Line 29:
 
  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 
  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 
|-
 
|-
|colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=spoIVFB_2855973_2856839_-1 Expression at a glance]'''&#160;&#160;&#160;{{PubMed|22383849}}<br/>[[Image:spoIVFB_expression.png|500px]]
+
|colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=spoIVFB_2855973_2856839_-1 Expression at a glance]'''&#160;&#160;&#160;{{PubMed|22383849}}<br/>[[Image:spoIVFB_expression.png|500px|link=http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU27970]]
 
|-
 
|-
 
|}
 
|}

Revision as of 14:09, 16 May 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

Original Publications

Ruanbao Zhou, Kangming Chen, Xianling Xiang, Liping Gu, Lee Kroos
Features of Pro-σK important for cleavage by SpoIVFB, an intramembrane metalloprotease.
J Bacteriol: 2013, 195(12);2793-806
[PubMed:23585539] [WorldCat.org] [DOI] (I p)

Ruanbao Zhou, Christina Cusumano, Dexin Sui, R Michael Garavito, Lee Kroos
Intramembrane proteolytic cleavage of a membrane-tethered transcription factor by a metalloprotease depends on ATP.
Proc Natl Acad Sci U S A: 2009, 106(38);16174-9
[PubMed:19805276] [WorldCat.org] [DOI] (I p)

Nathalie Campo, David Z Rudner
A branched pathway governing the activation of a developmental transcription factor by regulated intramembrane proteolysis.
Mol Cell: 2006, 23(1);25-35
[PubMed:16818230] [WorldCat.org] [DOI] (P p)

Leif Steil, Mónica Serrano, Adriano O Henriques, Uwe Völker
Genome-wide analysis of temporally regulated and compartment-specific gene expression in sporulating cells of Bacillus subtilis.
Microbiology (Reading): 2005, 151(Pt 2);399-420
[PubMed:15699190] [WorldCat.org] [DOI] (P p)

Patrick Eichenberger, Masaya Fujita, Shane T Jensen, Erin M Conlon, David Z Rudner, Stephanie T Wang, Caitlin Ferguson, Koki Haga, Tsutomu Sato, Jun S Liu, Richard Losick
The program of gene transcription for a single differentiating cell type during sporulation in Bacillus subtilis.
PLoS Biol: 2004, 2(10);e328
[PubMed:15383836] [WorldCat.org] [DOI] (I p)

Tran C Dong, Simon M Cutting
SpoIVB-mediated cleavage of SpoIVFA could provide the intercellular signal to activate processing of Pro-sigmaK in Bacillus subtilis.
Mol Microbiol: 2003, 49(5);1425-34
[PubMed:12940997] [WorldCat.org] [DOI] (P p)

David Z Rudner, Qi Pan, Richard M Losick
Evidence that subcellular localization of a bacterial membrane protein is achieved by diffusion and capture.
Proc Natl Acad Sci U S A: 2002, 99(13);8701-6
[PubMed:12060714] [WorldCat.org] [DOI] (P p)

David Z Rudner, Richard Losick
A sporulation membrane protein tethers the pro-sigmaK processing enzyme to its inhibitor and dictates its subcellular localization.
Genes Dev: 2002, 16(8);1007-18
[PubMed:11959848] [WorldCat.org] [DOI] (P p)

D Z Rudner, P Fawcett, R Losick
A family of membrane-embedded metalloproteases involved in regulated proteolysis of membrane-associated transcription factors.
Proc Natl Acad Sci U S A: 1999, 96(26);14765-70
[PubMed:10611287] [WorldCat.org] [DOI] (P p)

O Resnekov, R Losick
Negative regulation of the proteolytic activation of a developmental transcription factor in Bacillus subtilis.
Proc Natl Acad Sci U S A: 1998, 95(6);3162-7
[PubMed:9501233] [WorldCat.org] [DOI] (P p)

O Resnekov, S Alper, R Losick
Subcellular localization of proteins governing the proteolytic activation of a developmental transcription factor in Bacillus subtilis.
Genes Cells: 1996, 1(6);529-42
[PubMed:9078383] [WorldCat.org] [DOI] (P p)

E Ricca, S Cutting, R Losick
Characterization of bofA, a gene involved in intercompartmental regulation of pro-sigma K processing during sporulation in Bacillus subtilis.
J Bacteriol: 1992, 174(10);3177-84
[PubMed:1577688] [WorldCat.org] [DOI] (P p)

S Cutting, S Roels, R Losick
Sporulation operon spoIVF and the characterization of mutations that uncouple mother-cell from forespore gene expression in Bacillus subtilis.
J Mol Biol: 1991, 221(4);1237-56
[PubMed:1942049] [WorldCat.org] [DOI] (P p)