SpoIIE

• Description: protein serine phosphatase, septum-associated PP2C, dephosphorylation of SpoIIAA
  
  

Gene name	spoIIE
Synonyms	spoIIH, spoIIK
Essential	no
Product	protein serine phosphatase, septum-associated PP2C
Function	control of SigF activity required for normal formation of the asymmetric septum
Metabolic function and regulation of this protein in SubtiPathways: Stress
MW, pI	91 kDa, 6.137
Gene length, protein length	2481 bp, 827 aa
Immediate neighbours	trnSL-Glu1, yabS
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU00640

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: A phosphoprotein + H₂O = a protein + phosphate (according to Swiss-Prot) dephosphorylation of SpoIIAA

• Protein family: PP2C phosphatase

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions: SpoIIE-FtsZ, SpoIIE-SpoIIAB, SpoIIE-SpoIIE, SpoIIQ-SpoIIE

• Localization: cell membrane (according to Swiss-Prot)

Database entries

• Structure:

• Swiss prot entry: P37475

• KEGG entry: [3]

• E.C. number: 3.1.3.16

Expression and regulation

• Operon:

• Sigma factor:

• Regulation:
  • expressed under conditions that trigger sporulation (Spo0A) PubMed

• Regulatory mechanism:
  • Spo0A: transcription activation PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

Imrich Barak, Slovak Academy of Science, Bratislava, Slovakia homepage

References

Nathalie Campo, Kathleen A Marquis, David Z Rudner
SpoIIQ anchors membrane proteins on both sides of the sporulation septum in Bacillus subtilis.
J Biol Chem: 2008, 283(8);4975-82
[PubMed:18077456] [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)

Shonna M McBride, Aileen Rubio, Lei Wang, William G Haldenwang
Contributions of protein structure and gene position to the compartmentalization of the regulatory proteins sigma(E) and SpoIIE in sporulating Bacillus subtilis.
Mol Microbiol: 2005, 57(2);434-51
[PubMed:15978076] [WorldCat.org] [DOI] (P p)

Karen Carniol, Sigal Ben-Yehuda, Nicole King, Richard Losick
Genetic dissection of the sporulation protein SpoIIE and its role in asymmetric division in Bacillus subtilis.
J Bacteriol: 2005, 187(10);3511-20
[PubMed:15866939] [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)

Karen Carniol, Tae-Jong Kim, Chester W Price, Richard Losick
Insulation of the sigmaF regulatory system in Bacillus subtilis.
J Bacteriol: 2004, 186(13);4390-4
[PubMed:15205443] [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)

Andrea Feucht, Laura Abbotts, Jeffery Errington
The cell differentiation protein SpoIIE contains a regulatory site that controls its phosphatase activity in response to asymmetric septation.
Mol Microbiol: 2002, 45(4);1119-30
[PubMed:12180929] [WorldCat.org] [DOI] (P p)

Sigal Ben-Yehuda, Richard Losick
Asymmetric cell division in B. subtilis involves a spiral-like intermediate of the cytokinetic protein FtsZ.
Cell: 2002, 109(2);257-66
[PubMed:12007411] [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)

I Lucet, A Feucht, M D Yudkin, J Errington
Direct interaction between the cell division protein FtsZ and the cell differentiation protein SpoIIE.
EMBO J: 2000, 19(7);1467-75
[PubMed:10747015] [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)

I Lucet, R Borriss, M D Yudkin
Purification, kinetic properties, and intracellular concentration of SpoIIE, an integral membrane protein that regulates sporulation in Bacillus subtilis.
J Bacteriol: 1999, 181(10);3242-5
[PubMed:10322028] [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)

L J Wu, A Feucht, J Errington
Prespore-specific gene expression in Bacillus subtilis is driven by sequestration of SpoIIE phosphatase to the prespore side of the asymmetric septum.
Genes Dev: 1998, 12(9);1371-80
[PubMed:9573053] [WorldCat.org] [DOI] (P p)

A Khvorova, L Zhang, M L Higgins, P J Piggot
The spoIIE locus is involved in the Spo0A-dependent switch in the location of FtsZ rings in Bacillus subtilis.
J Bacteriol: 1998, 180(5);1256-60
[PubMed:9495766] [WorldCat.org] [DOI] (P p)

P A Levin, R Losick, P Stragier, F Arigoni
Localization of the sporulation protein SpoIIE in Bacillus subtilis is dependent upon the cell division protein FtsZ.
Mol Microbiol: 1997, 25(5);839-46
[PubMed:9364910] [WorldCat.org] [DOI] (P p)

K Pogliano, A E Hofmeister, R Losick
Disappearance of the sigma E transcription factor from the forespore and the SpoIIE phosphatase from the mother cell contributes to establishment of cell-specific gene expression during sporulation in Bacillus subtilis.
J Bacteriol: 1997, 179(10);3331-41
[PubMed:9150232] [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)

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)

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)

F Arigoni, K Pogliano, C D Webb, P Stragier, R Losick
Localization of protein implicated in establishment of cell type to sites of asymmetric division.
Science: 1995, 270(5236);637-40
[PubMed:7570022] [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)