Spo0F

• Description: phosphotransferase of the sporulation initiation phosphorelay
  
  

Gene name	spo0F
Synonyms
Essential	no
Product	phosphotransferase of the sporulation initiation phosphorelay
Function	initiation of sporulation
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 This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU37130

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions: Spo0F-Spo0E, RapA-Spo0F, Spo0F-RapB, Spo0F-KinA, Spo0F-Spo0B

• Localization: cytoplasm (according to Swiss-Prot)

Database entries

• Structure: 1SRR (phosphatase resistant mutant), 1F51 (complex with Spo0B), 2JVK (Mutant L66A), 2FSP

• UniProt: P06628

• KEGG entry: [3]

• E.C. number:

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:

References

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)

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 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)