CopZ

• 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 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

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

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

• Structure: 2QIF

• UniProt: O32221

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon: copZ-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

Timothy H Click, Sergei Y Ponomarev, George A Kaminski
Importance of electrostatic polarizability in calculating cysteine acidity constants and copper(I) binding energy of Bacillus subtilis CopZ.
J Comput Chem: 2012, 33(11);1142-51
[PubMed:22370900] [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)

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)

Liang Zhou, Chloe Singleton, Nick E Le Brun
High Cu(I) and low proton affinities of the CXXC motif of Bacillus subtilis CopZ.
Biochem J: 2008, 413(3);459-65
[PubMed:18419582] [WorldCat.org] [DOI] (I 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)