Difference between revisions of "AddB"
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= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
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=== Additional information=== | === Additional information=== | ||
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=The protein= | =The protein= | ||
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* '''Kinetic information:''' | * '''Kinetic information:''' | ||
| − | * '''Domains:''' | + | * '''[[Domains]]:''' |
* '''Modification:''' | * '''Modification:''' | ||
| − | * ''' | + | * '''[[Cofactors]]:''' |
* '''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=addB_1136320_1139820_1 addB] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=addB_1136320_1139820_1 addB] {{PubMed|22383849}} | ||
| − | * '''Sigma factor:''' [[SigA]] {{PubMed|7746142}} | + | * '''[[Sigma factor]]:''' [[SigA]] {{PubMed|7746142}} |
* '''Regulation:''' | * '''Regulation:''' | ||
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<pubmed> 23202527, 20116346 22933559</pubmed> | <pubmed> 23202527, 20116346 22933559</pubmed> | ||
==Original publications== | ==Original publications== | ||
| − | <pubmed>21809208,8387145,15610857,7746142, 19129187 1646786 10756102 9781875 17570399 20350930 22307084 22383849 21071401 23056615</pubmed> | + | <pubmed>21809208,8387145,15610857,7746142, 19129187 1646786 10756102 9781875 17570399 20350930 22307084 22383849 21071401 23056615 24682829 24670664</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 10:42, 2 April 2014
- Description: ATP-dependent deoxyribonuclease (subunit B)
| Gene name | addB |
| Synonyms | |
| Essential | no |
| Product | ATP-dependent deoxyribonuclease (subunit B)) |
| Function | DNA repair/ recombination |
| Gene expression levels in SubtiExpress: addB | |
| Interactions involving this protein in SubtInteract: AddB | |
| MW, pI | 134 kDa, 5.39 |
| Gene length, protein length | 3498 bp, 1166 aa |
| Immediate neighbours | yhjR, addA |
| Sequences | Protein DNA DNA_with_flanks |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
DNA repair/ recombination, genetic competence
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU10620
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- the enzyme is functional as a heterodimer of the AddA and AddB subunits, that it is a rapid and processive DNA helicase, and that it catalyses DNA unwinding using one single-stranded DNA motor of 3'→5' polarity located in the AddA subunit PubMed
- the AddB subunit contains a second putative ATP-binding pocket, but this does not contribute to the observed helicase activity and may instead be involved in the recognition of recombination hotspot sequences PubMed
- Protein family: uvrD-like helicase C-terminal domain (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
Database entries
- UniProt: P23477
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant: GP1106 (addAB, spc), available in Stülke lab
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
- Mark Dillingham, Bristol, U.K. (homepage)
Your additional remarks
References
Reviews
Dale B Wigley
Bacterial DNA repair: recent insights into the mechanism of RecBCD, AddAB and AdnAB.
Nat Rev Microbiol: 2013, 11(1);9-13
[PubMed:23202527]
[WorldCat.org]
[DOI]
(I p)
Justin S Lenhart, Jeremy W Schroeder, Brian W Walsh, Lyle A Simmons
DNA repair and genome maintenance in Bacillus subtilis.
Microbiol Mol Biol Rev: 2012, 76(3);530-64
[PubMed:22933559]
[WorldCat.org]
[DOI]
(I p)
Joseph T P Yeeles, Mark S Dillingham
The processing of double-stranded DNA breaks for recombinational repair by helicase-nuclease complexes.
DNA Repair (Amst): 2010, 9(3);276-85
[PubMed:20116346]
[WorldCat.org]
[DOI]
(I p)
Original publications
