Difference between revisions of "AddA"
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=Expression and regulation= | =Expression and regulation= | ||
− | * '''Operon:''' | + | * '''Operon:''' ''[[addB]]-[[addA]]'' {{PubMed|1646786}} |
− | * '''[[Sigma factor]]:''' | + | * '''[[Sigma factor]]:''' [[SigA]] {{PubMed|7746142}} |
* '''Regulation:''' | * '''Regulation:''' | ||
+ | ** positive control by [[ComK]] {{PubMed|7746142}} | ||
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
− | * '''Additional information:''' | + | * '''Additional information:''' |
=Biological materials = | =Biological materials = |
Revision as of 19:30, 18 September 2009
- Description: ATP-dependent deoxyribonuclease (subunit A)
Gene name | addA |
Synonyms | recE5 |
Essential | no |
Product | ATP-dependent deoxyribonuclease (subunit A)) |
Function | DNA repair and recombination |
MW, pI | 140 kDa, 5.127 |
Gene length, protein length | 3696 bp, 1232 aa |
Immediate neighbours | addB, sbcD |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU10630
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- 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:
- Interactions:
- Localization:
Database entries
- Structure:
- UniProt: P23478
- 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
Your additional remarks
References
Joseph T P Yeeles, Richard Cammack, Mark S Dillingham
An iron-sulfur cluster is essential for the binding of broken DNA by AddAB-type helicase-nucleases.
J Biol Chem: 2009, 284(12);7746-55
[PubMed:19129187]
[WorldCat.org]
[DOI]
(P p)
Alexander Serganov, Yu-Ren Yuan, Olga Pikovskaya, Anna Polonskaia, Lucy Malinina, Anh Tuân Phan, Claudia Hobartner, Ronald Micura, Ronald R Breaker, Dinshaw J Patel
Structural basis for discriminative regulation of gene expression by adenine- and guanine-sensing mRNAs.
Chem Biol: 2004, 11(12);1729-41
[PubMed:15610857]
[WorldCat.org]
[DOI]
(P p)
Etienne Dervyn, Marie-Françoise Noirot-Gros, Peggy Mervelet, Steven McGovern, S Dusko Ehrlich, Patrice Polard, Philippe Noirot
The bacterial condensin/cohesin-like protein complex acts in DNA repair and regulation of gene expression.
Mol Microbiol: 2004, 51(6);1629-40
[PubMed:15009890]
[WorldCat.org]
[DOI]
(P p)
B J Haijema, L W Hamoen, J Kooistra, G Venema, D van Sinderen
Expression of the ATP-dependent deoxyribonuclease of Bacillus subtilis is under competence-mediated control.
Mol Microbiol: 1995, 15(2);203-11
[PubMed:7746142]
[WorldCat.org]
[DOI]
(P p)
J Kooistra, B J Haijema, G Venema
The Bacillus subtilis addAB genes are fully functional in Escherichia coli.
Mol Microbiol: 1993, 7(6);915-23
[PubMed:8387145]
[WorldCat.org]
[DOI]
(P p)