Spo0B

• Description: sporulation initiation phosphotransferase of the phosphorelay
  
  

Gene name	spo0B
Synonyms	spo0D
Essential	no
Product	sporulation initiation phosphotransferase of the phosphorelay
Function	initiation of sporulation
Gene expression levels in SubtiExpress: spo0B
Interactions involving this protein in SubtInteract: Spo0B
Function and regulation of this protein in SubtiPathways: spo0B
MW, pI	22 kDa, 4.963
Gene length, protein length	576 bp, 192 aa
Immediate neighbours	obg, rpmA
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

phosphorelay, phosphoproteins

The gene

Basic information

• Locus tag: BSU27930

Phenotypes of a mutant

Arrest of sporulation at stage 0 (initiation) PubMed

Database entries

• BsubCyc: BSU27930

• 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:
  • Spo0B-Spo0F
  • Spo0B-Spo0A
  • YmcA-Spo0F PubMed

• Localization:

Database entries

• BsubCyc: BSU27930

• Structure: 1F51 (complex with Spo0F), 1IXM

• UniProt: P06535

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: spo0B-obg PubMed

• Expression browser: spo0B PubMed

• Sigma factor: SigA PubMed

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:
  • spo0B12, point mutation 85C>T (=R29W), available in BGSC 1S54
  • spo0B136, amber mutation 103A>T (=K35X), available in BGSC 1S16
  • spo0B580ts, point mutation 193G>A (=E65K), available in BGSC 1S90
  • spo0B581ts, point mutation 461G>A (=G154D), available in BGSC 1S91

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

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)

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)

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)

Masaya Fujita, Richard Losick
The master regulator for entry into sporulation in Bacillus subtilis becomes a cell-specific transcription factor after asymmetric division.
Genes Dev: 2003, 17(9);1166-74
[PubMed:12730135] [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)

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)

Y L Tzeng, X Z Zhou, J A Hoch
Phosphorylation of the Spo0B response regulator phosphotransferase of the phosphorelay initiating development in Bacillus subtilis.
J Biol Chem: 1998, 273(37);23849-55
[PubMed:9726997] [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)

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)

X Z Zhou, Madhusudan, J M Whiteley, J A Hoch, K I Varughese
Purification and preliminary crystallographic studies on the sporulation response regulatory phosphotransferase protein, Spo0B, from Bacillus subtilis.
Proteins: 1997, 27(4);597-600
[PubMed:9141138] [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)

K Trach, J A Hoch
The Bacillus subtilis spo0B stage 0 sporulation operon encodes an essential GTP-binding protein.
J Bacteriol: 1989, 171(3);1362-71
[PubMed:2537815] [WorldCat.org] [DOI] (P p)

P Zuber, R Losick
Role of AbrB in Spo0A- and Spo0B-dependent utilization of a sporulation promoter in Bacillus subtilis.
J Bacteriol: 1987, 169(5);2223-30
[PubMed:2437099] [WorldCat.org] [DOI] (P p)

F A Ferrari, K Trach, J A Hoch
Sequence analysis of the spo0B locus reveals a polycistronic transcription unit.
J Bacteriol: 1985, 161(2);556-62
[PubMed:3918016] [WorldCat.org] [DOI] (P p)