Copper homeostasis in Enterococcus hirae

FEMS Microbiol Rev. 2003 Jun;27(2-3):183-95. doi: 10.1016/S0168-6445(03)00053-6.


Copper is an essential component of life because of its convenient redox potential of 200-800 mV when bound to protein. Extensive insight into copper homeostasis has only emerged in the last decade and Enterococcus hirae has served as a paradigm for many aspects of the process. The cop operon of E. hirae regulates copper uptake, availability, and export. It consists of four genes that encode a repressor, CopY, a copper chaperone, CopZ, and two CPx-type copper ATPases, CopA and CopB. Most of these components have been conserved across the three evolutionary kingdoms. The four Cop proteins have been studied in vivo as well as in vitro and their function is understood in some detail.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adenosine Triphosphatases / genetics
  • Amino Acid Sequence
  • Arabidopsis Proteins*
  • Bacterial Proteins / metabolism
  • Copper / metabolism*
  • Enterococcus / metabolism*
  • Homeostasis
  • Ion Transport
  • Models, Genetic
  • Molecular Chaperones / genetics
  • Molecular Chaperones / metabolism
  • Repressor Proteins / metabolism
  • Sequence Alignment
  • Trans-Activators / metabolism


  • Arabidopsis Proteins
  • Bacterial Proteins
  • CCH protein, Arabidopsis
  • CopY protein, Enterococcus hirae
  • CopZ protein, Enterococcus hirae
  • Molecular Chaperones
  • Repressor Proteins
  • Trans-Activators
  • Copper
  • Adenosine Triphosphatases