Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae.

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Article

Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae.

The Journal of biological chemistry - 15 Jun 1993

Odermatt A, Suter H, Krapf R, Solioz M

Abstract excerpt

We cloned an operon, copAB, from Enterococcus hirae encoding two P-type ATPases of 727 and 745 amino acids, respectively. Both enzymes display heavy metal ion binding motifs in their polar N-terminal region. With an antibody against CopB, we showed on Western blots that expression of the operon i...

Topics

Adenosine Triphosphatases
Amino Acid Sequence
Base Sequence
Binding Sites
Carrier Proteins
Cation Transport Proteins
Cell Membrane
Cloning, Molecular
Copper
Copper Sulfate
Copper Transport Proteins
Copper-Transporting ATPases
DNA, Bacterial
Enterococcus
Genes, Bacterial
Homeostasis
Metals
Molecular Sequence Data

Source

Open in PubMed

Identifiers

PMID: 8048974

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8048974-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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