SpoIVFB

• 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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

• Interactions:
  • SpoIVFB-proSigK PubMed
  • SpoIVFB-BofA, to inhibit proteolytic activity of SpoIVFB PubMed
  • SpoIVFB-SpoIVFA, to facilitate the recruitment of BofA to SpoIVFB PubMed

• Localization:
  • integral membrane protein PubMed
  • outermost membrane surrounding the forespore PubMed

Database entries

• Structure:

• UniProt: P26937

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: spoIVFA-spoIVFB PubMed

• Expression browser: spoIVFB PubMed

• Sigma factor: SigE PubMed

• Regulation:
  • expressed early during sporulation in the mother cell (SigE, SpoIIID) PubMed

• Regulatory mechanism:
  • SpoIIID: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Original Publications

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)