Difference between revisions of "Spo0B"
| Line 40: | Line 40: | ||
| <br/><br/><br/><br/> | <br/><br/><br/><br/> | ||
| <br/><br/><br/><br/> | <br/><br/><br/><br/> | ||
| − | + | <br/><br/> | |
| − | |||
| − | |||
| − | |||
| − | |||
| = [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
| Line 99: | Line 95: | ||
| ** [[Spo0B]]-[[Spo0F]] | ** [[Spo0B]]-[[Spo0F]] | ||
| ** [[Spo0B]]-[[Spo0A]] | ** [[Spo0B]]-[[Spo0A]] | ||
| + | ** [[YmcA]]-[[Spo0F]] {{PubMed|23490197}} | ||
| * '''[[Localization]]:''' | * '''[[Localization]]:''' | ||
| Line 120: | Line 117: | ||
| * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=spo0B_2853981_2854559_-1 spo0B] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=spo0B_2853981_2854559_-1 spo0B] {{PubMed|22383849}} | ||
| − | * '''Sigma factor:''' [[SigA]] {{PubMed|2537815}} | + | * '''[[Sigma factor]]:''' [[SigA]] {{PubMed|2537815}} | 
| * '''Regulation:'''   | * '''Regulation:'''   | ||
| Line 151: | Line 148: | ||
| =References= | =References= | ||
| − | + | <pubmed>20413551 12730135,2437099,9141138,3918016,9299348,16788205,12067336,9726997,2118512, 10997904,1846779,9477965, 2537815 23490197</pubmed> | |
| − | <pubmed>20413551 12730135,2437099,9141138,3918016,9299348,16788205,12067336,9726997,2118512, 10997904,1846779,9477965, 2537815</pubmed> | ||
| [[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 12:54, 27 March 2013
-  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: Phosphorelay | |
| MW, pI | 22 kDa, 4.963 | 
| Gene length, protein length | 576 bp, 192 aa | 
| Immediate neighbours | obg, rpmA | 
| Get the DNA and protein sequences (Barbe et al., 2009) | |
| Genetic context    This image was kindly provided by SubtiList | |
| Expression at a glance   PubMed   | |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU27930
Phenotypes of a mutant
Arrest of sporulation at stage 0 (initiation) PubMed
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:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- UniProt: P06535
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- 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:
Labs working on this gene/protein
Your additional remarks
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)

