CopA

• 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

The gene

Basic information

• Locus tag: BSU33500

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

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:

• Interactions: CopA-CopZ

• Localization: cell membrane (according to Swiss-Prot)

Database entries

• Structure: 2RML ( N-terminal soluble domain)

• UniProt: O32220

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon: copZ-copA PubMed

• Sigma factor: SigA PubMed

• 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

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)

Gregory T Smaldone, John D Helmann
CsoR regulates the copper efflux operon copZA in Bacillus subtilis.
Microbiology (Reading): 2007, 153(Pt 12);4123-4128
[PubMed:18048925] [WorldCat.org] [DOI] (P p)

Irina M Solovieva, Karl-Dieter Entian
Metalloregulation in Bacillus subtilis: the copZ chromosomal gene is involved in cadmium resistance.
FEMS Microbiol Lett: 2004, 236(1);115-22
[PubMed:15212800] [WorldCat.org] [DOI] (P p)

Gilles P M Borrelly, Claudia A Blindauer, Ralf Schmid, Clive S Butler, Chris E Cooper, Ian Harvey, Peter J Sadler, Nigel J Robinson
A novel copper site in a cyanobacterial metallochaperone.
Biochem J: 2004, 378(Pt 2);293-7
[PubMed:14711369] [WorldCat.org] [DOI] (I p)

Ahmed Gaballa, Min Cao, John D Helmann
Two MerR homologues that affect copper induction of the Bacillus subtilis copZA operon.
Microbiology (Reading): 2003, 149(Pt 12);3413-3421
[PubMed:14663075] [WorldCat.org] [DOI] (P p)

Lucia Banci, Ivano Bertini, Simone Ciofi-Baffoni, Leonardo Gonnelli, Xun-Cheng Su
Structural basis for the function of the N-terminal domain of the ATPase CopA from Bacillus subtilis.
J Biol Chem: 2003, 278(50);50506-13
[PubMed:14514665] [WorldCat.org] [DOI] (P p)

Ahmed Gaballa, John D Helmann
Bacillus subtilis CPx-type ATPases: characterization of Cd, Zn, Co and Cu efflux systems.
Biometals: 2003, 16(4);497-505
[PubMed:12779235] [WorldCat.org] [DOI] (P p)

David S Radford, Margaret A Kihlken, Gilles P M Borrelly, Colin R Harwood, Nick E Le Brun, Jennifer S Cavet
CopZ from Bacillus subtilis interacts in vivo with a copper exporting CPx-type ATPase CopA.
FEMS Microbiol Lett: 2003, 220(1);105-12
[PubMed:12644235] [WorldCat.org] [DOI] (P p)

Lucia Banci, Ivano Bertini, Simone Ciofi-Baffoni, Rebecca Del Conte, Leonardo Gonnelli
Understanding copper trafficking in bacteria: interaction between the copper transport protein CopZ and the N-terminal domain of the copper ATPase CopA from Bacillus subtilis.
Biochemistry: 2003, 42(7);1939-49
[PubMed:12590580] [WorldCat.org] [DOI] (P p)

Lucia Banci, Ivano Bertini, Simone Ciofi-Baffoni, Mariapina D'Onofrio, Leonardo Gonnelli, Frutos Carlos Marhuenda-Egea, Francisco Javier Ruiz-Dueñas
Solution structure of the N-terminal domain of a potential copper-translocating P-type ATPase from Bacillus subtilis in the apo and Cu(I) loaded states.
J Mol Biol: 2002, 317(3);415-29
[PubMed:11922674] [WorldCat.org] [DOI] (P p)