Difference between revisions of "CopA"

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* '''Domains:'''  
 
* '''Domains:'''  
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** two N-terminal soluble domains, CopAa and CopAb, connected by a short linker
  
 
* '''Modification:'''
 
* '''Modification:'''
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==Original publications==
 
==Original publications==
 
'''Additional publications:''' {{PubMed|22077885}}
 
'''Additional publications:''' {{PubMed|22077885}}
<pubmed>19751213 11922674,12590580,14663075,12779235,12644235,18048925,14514665,14711369, 19378562 15212800  20233928</pubmed>
+
<pubmed>19751213 11922674,12590580,14663075,12779235,12644235,18048925,14514665,14711369, 19378562 15212800  20233928 22531974 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 09:22, 27 April 2012

  • Description: copper-transporting ATPase, resistance to copper

Gene name copA
Synonyms yvgX
Essential no
Product copper transporting ATPase
Function copper export, detoxification
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
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YvgX context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
CopA expression.png
























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

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:
    • two N-terminal soluble domains, CopAa and CopAb, connected by a short linker
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 2RML ( N-terminal soluble domain)
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • 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

Reviews

Original publications

Additional publications: PubMed

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)

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)