Spo0F

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  • Description: phosphotransferase of the sporulation initiation phosphorelay

Gene name spo0F
Synonyms
Essential no
Product phosphotransferase of the sporulation
initiation phosphorelay
Function initiation of sporulation
Interactions involving this protein in SubtInteract: Spo0F
Function and regulation of this protein in SubtiPathways:
Phosphorelay
MW, pI 14 kDa, 4.697
Gene length, protein length 372 bp, 124 aa
Immediate neighbours fbaA, ywjG
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
Spo0F context.gif
This image was kindly provided by SubtiList








Categories containing this gene/protein

phosphorelay, phosphoproteins

This gene is a member of the following regulons

SigH regulon, Spo0A regulon

The gene

Basic information

  • Locus tag: BSU37130

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:
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

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

Additional publications: PubMed

Alejandra R Diaz, Leighton J Core, Min Jiang, Michela Morelli, Christina H Chiang, Hendrik Szurmant, Marta Perego
Bacillus subtilis RapA phosphatase domain interaction with its substrate, phosphorylated Spo0F, and its inhibitor, the PhrA peptide.
J Bacteriol: 2012, 194(6);1378-88
[PubMed:22267516] [WorldCat.org] [DOI] (I p)

Prahathees Eswaramoorthy, Jeffrey Dinh, Daniel Duan, Oleg A Igoshin, Masaya Fujita
Single-cell measurement of the levels and distributions of the phosphorelay components in a population of sporulating Bacillus subtilis cells.
Microbiology (Reading): 2010, 156(Pt 8);2294-2304
[PubMed:20413551] [WorldCat.org] [DOI] (I p)

Wiep Klaas Smits, Cristina Bongiorni, Jan-Willem Veening, Leendert W Hamoen, Oscar P Kuipers, Marta Perego
Temporal separation of distinct differentiation pathways by a dual specificity Rap-Phr system in Bacillus subtilis.
Mol Microbiol: 2007, 65(1);103-20
[PubMed:17581123] [WorldCat.org] [DOI] (P p)

Patrick D McLaughlin, Benjamin G Bobay, Erin J Regel, Richele J Thompson, James A Hoch, John Cavanagh
Predominantly buried residues in the response regulator Spo0F influence specific sensor kinase recognition.
FEBS Lett: 2007, 581(7);1425-9
[PubMed:17350627] [WorldCat.org] [DOI] (P p)

Kottayil I Varughese, Igor Tsigelny, Haiyan Zhao
The crystal structure of beryllofluoride Spo0F in complex with the phosphotransferase Spo0B represents a phosphotransfer pretransition state.
J Bacteriol: 2006, 188(13);4970-7
[PubMed:16788205] [WorldCat.org] [DOI] (P p)

Douglas J Kojetin, Richele J Thompson, Linda M Benson, Stephen Naylor, Jenora Waterman, Keith G Davies, Charles H Opperman, Keith Stephenson, James A Hoch, John Cavanagh
Structural analysis of divalent metals binding to the Bacillus subtilis response regulator Spo0F: the possibility for in vitro metalloregulation in the initiation of sporulation.
Biometals: 2005, 18(5);449-66
[PubMed:16333746] [WorldCat.org] [DOI] (P p)

Sophie J Stephenson, Marta Perego
Interaction surface of the Spo0A response regulator with the Spo0E phosphatase.
Mol Microbiol: 2002, 44(6);1455-67
[PubMed:12067336] [WorldCat.org] [DOI] (P p)

Shu Ishikawa, Leighton Core, Marta Perego
Biochemical characterization of aspartyl phosphate phosphatase interaction with a phosphorylated response regulator and its inhibition by a pentapeptide.
J Biol Chem: 2002, 277(23);20483-9
[PubMed:11923303] [WorldCat.org] [DOI] (P p)

M Jiang, W Shao, M Perego, J A Hoch
Multiple histidine kinases regulate entry into stationary phase and sporulation in Bacillus subtilis.
Mol Microbiol: 2000, 38(3);535-42
[PubMed:11069677] [WorldCat.org] [DOI] (P p)

J Zapf, U Sen, Madhusudan, J A Hoch, K I Varughese
A transient interaction between two phosphorelay proteins trapped in a crystal lattice reveals the mechanism of molecular recognition and phosphotransfer in signal transduction.
Structure: 2000, 8(8);851-62
[PubMed:10997904] [WorldCat.org] [DOI] (P p)

M Jiang, Y L Tzeng, V A Feher, M Perego, J A Hoch
Alanine mutants of the Spo0F response regulator modifying specificity for sensor kinases in sporulation initiation.
Mol Microbiol: 1999, 33(2);389-95
[PubMed:10411754] [WorldCat.org] [DOI] (P p)

C Fabret, V A Feher, J A Hoch
Two-component signal transduction in Bacillus subtilis: how one organism sees its world.
J Bacteriol: 1999, 181(7);1975-83
[PubMed:10094672] [WorldCat.org] [DOI] (P p)

Y L Tzeng, V A Feher, J Cavanagh, M Perego, J A Hoch
Characterization of interactions between a two-component response regulator, Spo0F, and its phosphatase, RapB.
Biochemistry: 1998, 37(47);16538-45
[PubMed:9843420] [WorldCat.org] [DOI] (P p)

J Zapf, M Madhusudan, C E Grimshaw, J A Hoch, K I Varughese, J M Whiteley
A source of response regulator autophosphatase activity: the critical role of a residue adjacent to the Spo0F autophosphorylation active site.
Biochemistry: 1998, 37(21);7725-32
[PubMed:9601032] [WorldCat.org] [DOI] (P p)

V A Feher, Y L Tzeng, J A Hoch, J Cavanagh
Identification of communication networks in Spo0F: a model for phosphorylation-induced conformational change and implications for activation of multiple domain bacterial response regulators.
FEBS Lett: 1998, 425(1);1-6
[PubMed:9540996] [WorldCat.org] [DOI] (P p)

C E Grimshaw, S Huang, C G Hanstein, M A Strauch, D Burbulys, L Wang, J A Hoch, J M Whiteley
Synergistic kinetic interactions between components of the phosphorelay controlling sporulation in Bacillus subtilis.
Biochemistry: 1998, 37(5);1365-75
[PubMed:9477965] [WorldCat.org] [DOI] (P p)

M Madhusudan, J Zapf, J A Hoch, J M Whiteley, N H Xuong, K I Varughese
A response regulatory protein with the site of phosphorylation blocked by an arginine interaction: crystal structure of Spo0F from Bacillus subtilis.
Biochemistry: 1997, 36(42);12739-45
[PubMed:9335530] [WorldCat.org] [DOI] (P p)

Y L Tzeng, J A Hoch
Molecular recognition in signal transduction: the interaction surfaces of the Spo0F response regulator with its cognate phosphorelay proteins revealed by alanine scanning mutagenesis.
J Mol Biol: 1997, 272(2);200-12
[PubMed:9299348] [WorldCat.org] [DOI] (P p)

V A Feher, J W Zapf, J A Hoch, J M Whiteley, L P McIntosh, M Rance, N J Skelton, F W Dahlquist, J Cavanagh
High-resolution NMR structure and backbone dynamics of the Bacillus subtilis response regulator, Spo0F: implications for phosphorylation and molecular recognition.
Biochemistry: 1997, 36(33);10015-25
[PubMed:9254596] [WorldCat.org] [DOI] (P p)

Madhusudan, J Zapf, J M Whiteley, J A Hoch, N H Xuong, K I Varughese
Crystal structure of a phosphatase-resistant mutant of sporulation response regulator Spo0F from Bacillus subtilis.
Structure: 1996, 4(6);679-90
[PubMed:8805550] [WorldCat.org] [DOI] (P p)

Madhusudan, J Zapf, J M Whiteley, J A Hoch, N H Xuong, K I Varughese
Crystallization and preliminary X-ray analysis of a Y13S mutant of Spo0F from Bacillus subtilis.
Acta Crystallogr D Biol Crystallogr: 1996, 52(Pt 3);589-90
[PubMed:15299688] [WorldCat.org] [DOI] (P p)

J W Zapf, J A Hoch, J M Whiteley
A phosphotransferase activity of the Bacillus subtilis sporulation protein Spo0F that employs phosphoramidate substrates.
Biochemistry: 1996, 35(9);2926-33
[PubMed:8608130] [WorldCat.org] [DOI] (P p)

M Perego, P Glaser, J A Hoch
Aspartyl-phosphate phosphatases deactivate the response regulator components of the sporulation signal transduction system in Bacillus subtilis.
Mol Microbiol: 1996, 19(6);1151-7
[PubMed:8730857] [WorldCat.org] [DOI] (P p)

M Perego, J A Hoch
Cell-cell communication regulates the effects of protein aspartate phosphatases on the phosphorelay controlling development in Bacillus subtilis.
Proc Natl Acad Sci U S A: 1996, 93(4);1549-53
[PubMed:8643670] [WorldCat.org] [DOI] (P p)

K A Trach, J A Hoch
Multisensory activation of the phosphorelay initiating sporulation in Bacillus subtilis: identification and sequence of the protein kinase of the alternate pathway.
Mol Microbiol: 1993, 8(1);69-79
[PubMed:8497199] [WorldCat.org] [DOI] (P p)

M A Strauch, J J Wu, R H Jonas, J A Hoch
A positive feedback loop controls transcription of the spoOF gene, a component of the sporulation phosphorelay in Bacillus subtilis.
Mol Microbiol: 1993, 7(6);967-74
[PubMed:8483422] [WorldCat.org] [DOI] (P p)

M Predich, G Nair, I Smith
Bacillus subtilis early sporulation genes kinA, spo0F, and spo0A are transcribed by the RNA polymerase containing sigma H.
J Bacteriol: 1992, 174(9);2771-8
[PubMed:1569009] [WorldCat.org] [DOI] (P p)

D Burbulys, K A Trach, J A Hoch
Initiation of sporulation in B. subtilis is controlled by a multicomponent phosphorelay.
Cell: 1991, 64(3);545-52
[PubMed:1846779] [WorldCat.org] [DOI] (P p)

U Bai, M Lewandoski, E Dubnau, I Smith
Temporal regulation of the Bacillus subtilis early sporulation gene spo0F.
J Bacteriol: 1990, 172(9);5432-9
[PubMed:2118512] [WorldCat.org] [DOI] (P p)

M Perego, S P Cole, D Burbulys, K Trach, J A Hoch
Characterization of the gene for a protein kinase which phosphorylates the sporulation-regulatory proteins Spo0A and Spo0F of Bacillus subtilis.
J Bacteriol: 1989, 171(11);6187-96
[PubMed:2509430] [WorldCat.org] [DOI] (P p)

K Trach, J W Chapman, P Piggot, D LeCoq, J A Hoch
Complete sequence and transcriptional analysis of the spo0F region of the Bacillus subtilis chromosome.
J Bacteriol: 1988, 170(9);4194-208
[PubMed:2457578] [WorldCat.org] [DOI] (P p)

K A Trach, J W Chapman, P J Piggot, J A Hoch
Deduced product of the stage 0 sporulation gene spo0F shares homology with the Spo0A, OmpR, and SfrA proteins.
Proc Natl Acad Sci U S A: 1985, 82(21);7260-4
[PubMed:2997779] [WorldCat.org] [DOI] (P p)

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