Difference between revisions of "Spo0F"

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* '''Additional information:'''
 
* '''Additional information:'''
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium): 1508 {{PubMed|24696501}}
 +
** number of protein molecules per cell (complex medium with amino acids, without glucose): 750 {{PubMed|24696501}}
  
 
=Biological materials =
 
=Biological materials =

Revision as of 09:25, 17 April 2014

  • Description: phosphotransferase of the sporulation initiation phosphorelay

Gene name spo0F
Synonyms
Essential no
Product phosphotransferase of the sporulation
initiation phosphorelay
Function initiation of sporulation
Gene expression levels in SubtiExpress: spo0F
Interactions involving this protein in SubtInteract: Spo0F
Function and regulation of this protein in SubtiPathways:
spo0F
MW, pI 14 kDa, 4.697
Gene length, protein length 372 bp, 124 aa
Immediate neighbours fbaA, ywjG
Sequences Protein DNA DNA_with_flanks
Genetic context
Spo0F context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Spo0F expression.png















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:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 1508 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 750 PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Vijay Parashar, Melissa A Konkol, Daniel B Kearns, Matthew B Neiditch
A plasmid-encoded phosphatase regulates Bacillus subtilis biofilm architecture, sporulation, and genetic competence.
J Bacteriol: 2013, 195(10);2437-48
[PubMed:23524609] [WorldCat.org] [DOI] (I p)

Valerie J Carabetta, Andrew W Tanner, Todd M Greco, Melissa Defrancesco, Ileana M Cristea, David Dubnau
A complex of YlbF, YmcA and YaaT regulates sporulation, competence and biofilm formation by accelerating the phosphorylation of Spo0A.
Mol Microbiol: 2013, 88(2);283-300
[PubMed:23490197] [WorldCat.org] [DOI] (I p)

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)

Vijay Parashar, Nicolas Mirouze, David A Dubnau, Matthew B Neiditch
Structural basis of response regulator dephosphorylation by Rap phosphatases.
PLoS Biol: 2011, 9(2);e1000589
[PubMed:21346797] [WorldCat.org] [DOI] (I e)

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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