Difference between revisions of "AddB"
Line 99: | Line 99: | ||
=== Database entries === | === Database entries === | ||
− | * '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1Y26 1Y26] (the [[riboswitch]] in complex with adenine) | + | * '''Structure:''' |
+ | ** [http://www.rcsb.org/pdb/explore/explore.do?structureId=3U4Q 3U4Q] (the [[AddA]]-[[AddB]]-DNA complex) {{PubMed|22307084}} | ||
+ | ** [http://www.rcsb.org/pdb/explore.do?structureId=1Y26 1Y26] (the [[riboswitch]] in complex with adenine) | ||
* '''UniProt:''' [http://www.uniprot.org/uniprot/P23477 P23477] | * '''UniProt:''' [http://www.uniprot.org/uniprot/P23477 P23477] | ||
Line 148: | Line 150: | ||
==Original publications== | ==Original publications== | ||
'''Additional publications:''' {{PubMed|21071401}} | '''Additional publications:''' {{PubMed|21071401}} | ||
− | <pubmed>21809208,8387145,15610857,7746142, 19129187 1646786 10756102 9781875 17570399 20350930 </pubmed> | + | <pubmed>21809208,8387145,15610857,7746142, 19129187 1646786 10756102 9781875 17570399 20350930 22307084</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 17:26, 4 May 2012
- Description: ATP-dependent deoxyribonuclease (subunit B)
Gene name | addB |
Synonyms | |
Essential | no |
Product | ATP-dependent deoxyribonuclease (subunit B)) |
Function | DNA repair/ recombination |
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 |
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
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:
- Domains:
- Modification:
- Cofactor(s):
- 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
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
Additional publications: PubMed