Difference between revisions of "CopZ"

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|style="background:#ABCDEF;" align="center"|'''Function''' || resistance to copper
 
|style="background:#ABCDEF;" align="center"|'''Function''' || resistance to copper
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/CopZ CopZ]
 
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://cellpublisher.gobics.de/view/GqbblRJkBH metal ion homeostasis]'''
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://cellpublisher.gobics.de/view/GqbblRJkBH metal ion homeostasis]'''

Revision as of 09:32, 7 August 2011

  • Description: copper transport protein, metallochaperone

Gene name copZ
Synonyms yvgY
Essential no
Product copper transport protein, metallochaperone
Function resistance to copper
Interactions involving this protein in SubtInteract: CopZ
Metabolic function and regulation of this protein in SubtiPathways:
metal ion homeostasis
MW, pI 7 kDa, 4.162
Gene length, protein length 207 bp, 69 aa
Immediate neighbours copA, csoR
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YvgY context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

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

This gene is a member of the following regulons

CsoR regulon

The gene

Basic information

  • Locus tag: BSU33510

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s): carries a tetranuclear Cu(I) cluster (as [Cu4(S-Cys)4(N-His)2] cluster) PubMed
  • Effectors of protein activity:
  • Interactions: CopA-CopZ, for the transfer of the Cu(I) cluster PubMed
  • Localization: cytoplasm (according to Swiss-Prot)

Database entries

  • 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

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)

Stephen Hearnshaw, Claire West, Chloe Singleton, Liang Zhou, Margaret A Kihlken, Richard W Strange, Nick E Le Brun, Andrew M Hemmings
A tetranuclear Cu(I) cluster in the metallochaperone protein CopZ.
Biochemistry: 2009, 48(40);9324-6
[PubMed:19746989] [WorldCat.org] [DOI] (I p)

Agustina Rodriguez-Granillo, Pernilla Wittung-Stafshede
Tuning of copper-loop flexibility in Bacillus subtilis CopZ copper chaperone: role of conserved residues.
J Phys Chem B: 2009, 113(7);1919-32
[PubMed:19170606] [WorldCat.org] [DOI] (P p)

Agustina Rodriguez-Granillo, Pernilla Wittung-Stafshede
Structure and dynamics of Cu(I) binding in copper chaperones Atox1 and CopZ: a computer simulation study.
J Phys Chem B: 2008, 112(15);4583-93
[PubMed:18361527] [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)