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

Markus Mastny, Alexander Heuck, Robert Kurzbauer, Anja Heiduk, Prisca Boisguerin, Rudolf Volkmer, Michael Ehrmann, Christopher D A Rodrigues, David Z Rudner, Tim Clausen
CtpB assembles a gated protease tunnel regulating cell-cell signaling during spore formation in Bacillus subtilis.
Cell: 2013, 155(3);647-58
[PubMed:24243021] [WorldCat.org] [DOI] (I p)

Yang Zhang, Paul M Luethy, Ruanbao Zhou, Lee Kroos
Residues in conserved loops of intramembrane metalloprotease SpoIVFB interact with residues near the cleavage site in pro-σK.
J Bacteriol: 2013, 195(21);4936-46
[PubMed:23995631] [WorldCat.org] [DOI] (I p)

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)

Ruanbao Zhou, Lee Kroos
BofA protein inhibits intramembrane proteolysis of pro-sigmaK in an intercompartmental signaling pathway during Bacillus subtilis sporulation.
Proc Natl Acad Sci U S A: 2004, 101(17);6385-90
[PubMed:15087499] [WorldCat.org] [DOI] (P 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)