CopA

• Description: copper-transporting ATPase, resistance to copper
  
  

Gene name	copA
Synonyms	yvgX
Essential	no
Product	copper transporting ATPase
Function	copper export, detoxification
Gene expression levels in SubtiExpress: copA
Interactions involving this protein in SubtInteract: CopA
Metabolic function and regulation of this protein in SubtiPathways: metal ion homeostasis
MW, pI	85 kDa, 5.484
Gene length, protein length	2409 bp, 803 aa
Immediate neighbours	cadA, copZ
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

transporters/ other, trace metal homeostasis (Cu, Zn, Ni, Mn, Mo), resistance against toxic metals, membrane proteins

This gene is a member of the following regulons

CsoR regulon

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:
  • two N-terminal soluble domains, CopAa and CopAb, connected by a short linker

• Modification:

• Cofactors:

• Effectors of protein activity:

• Interactions:
  • CopA-CopZ, for the transfer of the Cu(I) cluster PubMed

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

Database entries

• Structure:
  • 2RML ( N-terminal soluble domain)
  • 4BBJ (the protein from Legionella pneumophila, 45% identity, 79% similarity) PubMed

• UniProt: O32220

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon: copZ-copA PubMed

• Expression browser: copA PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • induced by copper (CsoR) PubMed

• Regulatory mechanism:
  • CsoR: transcription repression PubMed

• 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

Reviews

Amy C Rosenzweig, José M Argüello
Toward a molecular understanding of metal transport by P(1B)-type ATPases.
Curr Top Membr: 2012, 69;113-36
[PubMed:23046649] [WorldCat.org] [DOI] (I p)

Amie K Boal, Amy C Rosenzweig
Structural biology of copper trafficking.
Chem Rev: 2009, 109(10);4760-79
[PubMed:19824702] [WorldCat.org] [DOI] (I p)

Original publications

Magnus Andersson, Daniel Mattle, Oleg Sitsel, Tetyana Klymchuk, Anna Marie Nielsen, Lisbeth Birk Møller, Stephen H White, Poul Nissen, Pontus Gourdon
Copper-transporting P-type ATPases use a unique ion-release pathway.
Nat Struct Mol Biol: 2014, 21(1);43-8
[PubMed:24317491] [WorldCat.org] [DOI] (I p)

Liang Zhou, Chloe Singleton, Nick E Le Brun
CopAb, the second N-terminal soluble domain of Bacillus subtilis CopA, dominates the Cu(I)-binding properties of CopAab.
Dalton Trans: 2012, 41(19);5939-48
[PubMed:22531974] [WorldCat.org] [DOI] (I p)

Liang Zhou, Chloe Singleton, Oliver Hecht, Geoffrey R Moore, Nick E Le Brun
Cu(I)- and proton-binding properties of the first N-terminal soluble domain of Bacillus subtilis CopA.
FEBS J: 2012, 279(2);285-98
[PubMed:22077885] [WorldCat.org] [DOI] (I p)

Shashi Chillappagari, Andreas Seubert, Hein Trip, Oscar P Kuipers, Mohamed A Marahiel, Marcus Miethke
Copper stress affects iron homeostasis by destabilizing iron-sulfur cluster formation in Bacillus subtilis.
J Bacteriol: 2010, 192(10);2512-24
[PubMed:20233928] [WorldCat.org] [DOI] (I p)

Chloe Singleton, Stephen Hearnshaw, Liang Zhou, Nick E Le Brun, Andrew M Hemmings
Mechanistic insights into Cu(I) cluster transfer between the chaperone CopZ and its cognate Cu(I)-transporting P-type ATPase, CopA.
Biochem J: 2009, 424(3);347-56
[PubMed:19751213] [WorldCat.org] [DOI] (I e)

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)