Difference between revisions of "CopA"
Line 52: | Line 52: | ||
=== Basic information/ Evolution === | === Basic information/ Evolution === | ||
− | * '''Catalyzed reaction/ biological activity:''' | + | * '''Catalyzed reaction/ biological activity:''' ATP + H<sub>2</sub>O + Cu<sup>1+</sup>(In) = ADP + phosphate + Cu<sup>1+</sup>(Out) (according to Swiss-Prot) |
* '''Protein family:''' Type IB subfamily (according to Swiss-Prot) | * '''Protein family:''' Type IB subfamily (according to Swiss-Prot) |
Revision as of 14:08, 24 May 2009
- Description: copper-transporting ATPase, resistance to copper
Gene name | copA |
Synonyms | yvgX |
Essential | no |
Product | copper transporting ATPase |
Function | copper export |
MW, pI | 85 kDa, 5.484 |
Gene length, protein length | 2409 bp, 803 aa |
Immediate neighbours | cadA, copZ |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Coordinates:
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP + H2O + Cu1+(In) = ADP + phosphate + Cu1+(Out) (according to Swiss-Prot)
- Protein family: Type IB subfamily (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: cell membrane (according to Swiss-Prot)
Database entries
- Structure: 2RML ( N-terminal soluble domain)
- Swiss prot entry: O32220
- KEGG entry: BSU33500
- E.C. number:
Additional information
Expression and regulation
- Regulation: induced by copper PubMed
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
John Helmann, Cornell University, USA Homepage
Your additional remarks
References
Chloe Singleton, Nick E Le Brun
The N-terminal soluble domains of Bacillus subtilis CopA exhibit a high affinity and capacity for Cu(I) ions.
Dalton Trans: 2009, (4);688-96
[PubMed:19378562]
[WorldCat.org]
[DOI]
(P p)
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed