Difference between revisions of "SplB"
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* '''Cofactor(s):''' | * '''Cofactor(s):''' | ||
| − | ** contains a [4Fe-4S] cluster | + | ** contains a [4Fe-4S] cluster, uses the [4Fe-4S] cluster to reduce SAM |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=splB_1461770_1462798_1 splB] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=splB_1461770_1462798_1 splB] {{PubMed|22383849}} | ||
| − | * '''Sigma factor:''' [[SigG]] {{PubMed|15699190,8021181}} | + | * '''[[Sigma factor]]:''' [[SigG]] {{PubMed|15699190,8021181}} |
* '''Regulation:''' expressed during sporulation in the forespore ([[SigG]]) {{PubMed|16497325}} | * '''Regulation:''' expressed during sporulation in the forespore ([[SigG]]) {{PubMed|16497325}} | ||
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=References= | =References= | ||
| − | <pubmed> 15699190,8021181 21671623 22197590</pubmed> | + | <pubmed> 15699190,8021181 21671623 22197590 23607538 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 12:41, 26 April 2013
- Description: spore photoproduct lyase
| Gene name | splB |
| Synonyms | spl |
| Essential | no |
| Product | spore photoproduct lyase |
| Function | protection of spore DNA against photodamage |
| Gene expression levels in SubtiExpress: splB | |
| MW, pI | 39 kDa, 8.524 |
| Gene length, protein length | 1026 bp, 342 aa |
| Immediate neighbours | splA, ykwB |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
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Expression at a glance PubMed
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Contents
Categories containing this gene/protein
DNA repair/ recombination, sporulation proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU13930
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- repairs a special thymine dimer (5-thyminyl-5,6-dihydrothymine), which is commonly called spore photoproduct at the early germination phase
- 5-thyminyl-5,6-dihydrothymine (in DNA) = 2 thymine residues (in DNA) (according to Swiss-Prot)
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- contains a [4Fe-4S] cluster, uses the [4Fe-4S] cluster to reduce SAM
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: P37956
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Additional information:
Biological materials
- Mutant: BP130 (del splB::spc), available in Fabian Commichau's lab
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Linlin Yang, Renae S Nelson, Alhosna Benjdia, Gengjie Lin, Joshua Telser, Stefan Stoll, Ilme Schlichting, Lei Li
A radical transfer pathway in spore photoproduct lyase.
Biochemistry: 2013, 52(18);3041-50
[PubMed:23607538]
[WorldCat.org]
[DOI]
(I p)
Lei Li
Mechanistic studies of the radical SAM enzyme spore photoproduct lyase (SPL).
Biochim Biophys Acta: 2012, 1824(11);1264-77
[PubMed:22197590]
[WorldCat.org]
[DOI]
(P p)
Linlin Yang, Gengjie Lin, Degang Liu, Karl J Dria, Joshua Telser, Lei Li
Probing the reaction mechanism of spore photoproduct lyase (SPL) via diastereoselectively labeled dinucleotide SP TpT substrates.
J Am Chem Soc: 2011, 133(27);10434-47
[PubMed:21671623]
[WorldCat.org]
[DOI]
(I p)
Leif Steil, Mónica Serrano, Adriano O Henriques, Uwe Völker
Genome-wide analysis of temporally regulated and compartment-specific gene expression in sporulating cells of Bacillus subtilis.
Microbiology (Reading): 2005, 151(Pt 2);399-420
[PubMed:15699190]
[WorldCat.org]
[DOI]
(P p)
M Pedraza-Reyes, F Gutiérrez-Corona, W L Nicholson
Temporal regulation and forespore-specific expression of the spore photoproduct lyase gene by sigma-G RNA polymerase during Bacillus subtilis sporulation.
J Bacteriol: 1994, 176(13);3983-91
[PubMed:8021181]
[WorldCat.org]
[DOI]
(P p)
