SpoIIAA

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  • Description: anti-anti-SigF

Gene name spoIIAA
Synonyms
Essential no
Product anti-anti-SigF
Function control of SigF activity
Gene expression levels in SubtiExpress: spoIIAA
Interactions involving this protein in SubtInteract: SpoIIAA
Metabolic function and regulation of this protein in SubtiPathways:
spoIIAA
MW, pI 12 kDa, 5.855
Gene length, protein length 351 bp, 117 aa
Immediate neighbours spoIIAB, dacF
Sequences Protein DNA DNA_with_flanks
Genetic context
SpoIIAA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SpoIIAA expression.png















Categories containing this gene/protein

sigma factors and their control, sporulation proteins, phosphoproteins

This gene is a member of the following regulons

AbrB regulon, SigF regulon, SigG regulon, SigH regulon, SinR regulon, Spo0A regulon

The gene

Basic information

  • Locus tag: BSU23470

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: anti-sigma-factor antagonist family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 1TIL (complex with SpoIIAB, Geobacillus stearothermophilus), 1AUZ (NMR)
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation: repressed by glucose (5.2-fold) PubMed, dacF: expressed during sporulation, spoIIAA: expressed early during sporulation
    • expressed under conditions that trigger sporulation (Spo0A) PubMed
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 388 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 237 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 3471 PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Modeling of SigF activation

Original Publications

Onuma Chumsakul, Hiroki Takahashi, Taku Oshima, Takahiro Hishimoto, Shigehiko Kanaya, Naotake Ogasawara, Shu Ishikawa
Genome-wide binding profiles of the Bacillus subtilis transition state regulator AbrB and its homolog Abh reveals their interactive role in transcriptional regulation.
Nucleic Acids Res: 2011, 39(2);414-28
[PubMed:20817675] [WorldCat.org] [DOI] (I p)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)

Oleg A Igoshin, Chester W Price, Michael A Savageau
Signalling network with a bistable hysteretic switch controls developmental activation of the sigma transcription factor in Bacillus subtilis.
Mol Microbiol: 2006, 61(1);165-84
[PubMed:16824103] [WorldCat.org] [DOI] (P p)

Alain Lévine, Françoise Vannier, Cédric Absalon, Lauriane Kuhn, Peter Jackson, Elaine Scrivener, Valérie Labas, Joëlle Vinh, Patrick Courtney, Jérôme Garin, Simone J Séror
Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes.
Proteomics: 2006, 6(7);2157-73
[PubMed:16493705] [WorldCat.org] [DOI] (P p)

Masaya Fujita, José Eduardo González-Pastor, Richard Losick
High- and low-threshold genes in the Spo0A regulon of Bacillus subtilis.
J Bacteriol: 2005, 187(4);1357-68
[PubMed:15687200] [WorldCat.org] [DOI] (P p)

Joanna Clarkson, Iain D Campbell, Michael D Yudkin
Efficient regulation of sigmaF, the first sporulation-specific sigma factor in B.subtilis.
J Mol Biol: 2004, 342(4);1187-95
[PubMed:15351644] [WorldCat.org] [DOI] (P p)

Joanna Clarkson, Iain D Campbell, Michael D Yudkin
Physical evidence for the induced release of the Bacillus subtilis transcription factor, sigma(F), from its inhibitory complex.
J Mol Biol: 2004, 340(2);203-9
[PubMed:15201047] [WorldCat.org] [DOI] (P p)

Joanna Clarkson, Jwu-Ching Shu, David A Harris, Iain D Campbell, Michael D Yudkin
Fluorescence and kinetic analysis of the SpoIIAB phosphorylation reaction, a key regulator of sporulation in Bacillus subtilis.
Biochemistry: 2004, 43(11);3120-8
[PubMed:15023063] [WorldCat.org] [DOI] (P p)

Karen Carniol, Patrick Eichenberger, Richard Losick
A threshold mechanism governing activation of the developmental regulatory protein sigma F in Bacillus subtilis.
J Biol Chem: 2004, 279(15);14860-70
[PubMed:14744853] [WorldCat.org] [DOI] (P p)

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135] [WorldCat.org] [DOI] (P p)

Margaret S Ho, Karen Carniol, Richard Losick
Evidence in support of a docking model for the release of the transcription factor sigma F from the antisigma factor SpoIIAB in Bacillus subtilis.
J Biol Chem: 2003, 278(23);20898-905
[PubMed:12676949] [WorldCat.org] [DOI] (P p)

J Clarkson, I D Campbell, M D Yudkin
NMR studies of the interactions of SpoIIAA with its partner proteins that regulate sporulation in Bacillus subtilis.
J Mol Biol: 2001, 314(3);359-64
[PubMed:11846550] [WorldCat.org] [DOI] (P p)

Q Pan, D A Garsin, R Losick
Self-reinforcing activation of a cell-specific transcription factor by proteolysis of an anti-sigma factor in B. subtilis.
Mol Cell: 2001, 8(4);873-83
[PubMed:11684022] [WorldCat.org] [DOI] (P p)

C S Lee, J Clarkson, J C Shu, I D Campbell, M D Yudkin
Bacillus subtilis mutations that alter the pathway of phosphorylation of the anti-anti-sigmaF factor SpoIIAA lead to a Spo- phenotype.
Mol Microbiol: 2001, 40(1);9-19
[PubMed:11298272] [WorldCat.org] [DOI] (P p)

A Feucht, R A Daniel, J Errington
Characterization of a morphological checkpoint coupling cell-specific transcription to septation in Bacillus subtilis.
Mol Microbiol: 1999, 33(5);1015-26
[PubMed:10476035] [WorldCat.org] [DOI] (P p)

N King, O Dreesen, P Stragier, K Pogliano, R Losick
Septation, dephosphorylation, and the activation of sigmaF during sporulation in Bacillus subtilis.
Genes Dev: 1999, 13(9);1156-67
[PubMed:10323866] [WorldCat.org] [DOI] (P p)

N Frandsen, I Barák, C Karmazyn-Campelli, P Stragier
Transient gene asymmetry during sporulation and establishment of cell specificity in Bacillus subtilis.
Genes Dev: 1999, 13(4);394-9
[PubMed:10049355] [WorldCat.org] [DOI] (P p)

D A Garsin, L Duncan, D M Paskowitz, R Losick
The kinase activity of the antisigma factor SpoIIAB is required for activation as well as inhibition of transcription factor sigmaF during sporulation in Bacillus subtilis.
J Mol Biol: 1998, 284(3);569-78
[PubMed:9826499] [WorldCat.org] [DOI] (P p)

D A Garsin, D M Paskowitz, L Duncan, R Losick
Evidence for common sites of contact between the antisigma factor SpoIIAB and its partners SpoIIAA and the developmental transcription factor sigmaF in Bacillus subtilis.
J Mol Biol: 1998, 284(3);557-68
[PubMed:9826498] [WorldCat.org] [DOI] (P p)

P J Lewis, L J Wu, J Errington
Establishment of prespore-specific gene expression in Bacillus subtilis: localization of SpoIIE phosphatase and initiation of compartment-specific proteolysis.
J Bacteriol: 1998, 180(13);3276-84
[PubMed:9642177] [WorldCat.org] [DOI] (P p)

M Lord, T Magnin, M D Yudkin
Protein conformational change and nucleotide binding involved in regulation of sigmaF in Bacillus subtilis.
J Bacteriol: 1996, 178(23);6730-5
[PubMed:8955289] [WorldCat.org] [DOI] (P p)

S M Najafi, D A Harris, M D Yudkin
The SpoIIAA protein of Bacillus subtilis has GTP-binding properties.
J Bacteriol: 1996, 178(22);6632-4
[PubMed:8932322] [WorldCat.org] [DOI] (P p)

P J Lewis, T Magnin, J Errington
Compartmentalized distribution of the proteins controlling the prespore-specific transcription factor sigmaF of Bacillus subtilis.
Genes Cells: 1996, 1(10);881-94
[PubMed:9077448] [WorldCat.org] [DOI] (P p)

S Alper, A Dufour, D A Garsin, L Duncan, R Losick
Role of adenosine nucleotides in the regulation of a stress-response transcription factor in Bacillus subtilis.
J Mol Biol: 1996, 260(2);165-77
[PubMed:8764398] [WorldCat.org] [DOI] (P p)

L Duncan, S Alper, R Losick
SpoIIAA governs the release of the cell-type specific transcription factor sigma F from its anti-sigma factor SpoIIAB.
J Mol Biol: 1996, 260(2);147-64
[PubMed:8764397] [WorldCat.org] [DOI] (P p)

F Arigoni, L Duncan, S Alper, R Losick, P Stragier
SpoIIE governs the phosphorylation state of a protein regulating transcription factor sigma F during sporulation in Bacillus subtilis.
Proc Natl Acad Sci U S A: 1996, 93(8);3238-42
[PubMed:8622920] [WorldCat.org] [DOI] (P p)

A Feucht, T Magnin, M D Yudkin, J Errington
Bifunctional protein required for asymmetric cell division and cell-specific transcription in Bacillus subtilis.
Genes Dev: 1996, 10(7);794-803
[PubMed:8846916] [WorldCat.org] [DOI] (P p)

T Magnin, M Lord, J Errington, M D Yudkin
Establishing differential gene expression in sporulating Bacillus subtilis: phosphorylation of SpoIIAA (anti-anti-sigmaF) alters its conformation and prevents formation of a SpoIIAA/SpoIIAB/ADP complex.
Mol Microbiol: 1996, 19(4);901-7
[PubMed:8820658] [WorldCat.org] [DOI] (P p)

L Duncan, S Alper, F Arigoni, R Losick, P Stragier
Activation of cell-specific transcription by a serine phosphatase at the site of asymmetric division.
Science: 1995, 270(5236);641-4
[PubMed:7570023] [WorldCat.org] [DOI] (P p)

S Alper, L Duncan, R Losick
An adenosine nucleotide switch controlling the activity of a cell type-specific transcription factor in B. subtilis.
Cell: 1994, 77(2);195-205
[PubMed:8168129] [WorldCat.org] [DOI] (P p)

K T Min, C M Hilditch, B Diederich, J Errington, M D Yudkin
Sigma F, the first compartment-specific transcription factor of B. subtilis, is regulated by an anti-sigma factor that is also a protein kinase.
Cell: 1993, 74(4);735-42
[PubMed:8358793] [WorldCat.org] [DOI] (P p)

T Bird, D Burbulys, J J Wu, M A Strauch, J A Hoch, G B Spiegelman
The effect of supercoiling on the in vitro transcription of the spoIIA operon from Bacillus subtilis.
Biochimie: 1992, 74(7-8);627-34
[PubMed:1391042] [WorldCat.org] [DOI] (P p)

K York, T J Kenney, S Satola, C P Moran, H Poth, P Youngman
Spo0A controls the sigma A-dependent activation of Bacillus subtilis sporulation-specific transcription unit spoIIE.
J Bacteriol: 1992, 174(8);2648-58
[PubMed:1556084] [WorldCat.org] [DOI] (P p)

P Margolis, A Driks, R Losick
Establishment of cell type by compartmentalized activation of a transcription factor.
Science: 1991, 254(5031);562-5
[PubMed:1948031] [WorldCat.org] [DOI] (P p)

R Schmidt, P Margolis, L Duncan, R Coppolecchia, C P Moran, R Losick
Control of developmental transcription factor sigma F by sporulation regulatory proteins SpoIIAA and SpoIIAB in Bacillus subtilis.
Proc Natl Acad Sci U S A: 1990, 87(23);9221-5
[PubMed:2123551] [WorldCat.org] [DOI] (P p)

J Errington, J Mandelstam
Use of a lacZ gene fusion to determine the dependence pattern of sporulation operon spoIIA in spo mutants of Bacillus subtilis.
J Gen Microbiol: 1986, 132(11);2967-76
[PubMed:3114419] [WorldCat.org] [DOI] (P p)

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