U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

copA Cu(+) exporting P-type ATPase;soluble Cu(+) chaperone [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 946106, updated on 4-Feb-2026
Official Symbol
copA
Official Full Name
Cu(+) exporting P-type ATPase;soluble Cu(+) chaperone
Primary source
ECOCYC:G6260
Locus tag
b0484
See related
ASAP:ABE-0001681
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK0478; ybaR
Summary
Upregulated by GSNO in defined medium (anaerobic). [More information is available at EcoGene: EG13246]. CopA is a member of the P-type ATPase cation transporter family and is involved in copper homeostasis as an ATP-dependent exporter of monovalent copper under primarily aerobic conditions . [More information is available at EcoCyc: G6260].
Try the new Gene page
Try the new Transcripts and proteins table
Sequence:
NC_000913.3 (508875..511379, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene ncRNA Neighboring gene TraB family protein YbaP Neighboring gene DNA-binding transcriptional regulator YbaQ Neighboring gene glutaminase 1 Neighboring gene putative transporter YbaT

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Programmed Ribosomal Frameshifting Generates a Copper Transporter and a Copper Chaperone from the Same Gene. Meydan S, et al. Mol Cell, 2017 Jan 19. PMID 28107647, Free PMC Article
  2. Distinct functions of serial metal-binding domains in the Escherichia coli P1 B -ATPase CopA. Drees SL, et al. Mol Microbiol, 2015 Aug. PMID 25899340
  3. P-type ATPases of eukaryotes and bacteria: sequence analyses and construction of phylogenetic trees. Fagan MJ, et al. J Mol Evol, 1994 Jan. PMID 8151716
  4. CopA: An Escherichia coli Cu(I)-translocating P-type ATPase. Rensing C, et al. Proc Natl Acad Sci U S A, 2000 Jan 18. PMID 10639134, Free PMC Article
  5. Biochemical characterization of CopA, the Escherichia coli Cu(I)-translocating P-type ATPase. Fan B, et al. J Biol Chem, 2002 Dec 6. PMID 12351646

See all (33) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. CopA chaperone is expressed in E. coli from the same gene that encodes the transporter. Some ribosomes translating copA undergo programmed frameshifting, terminate translation in the -1 frame, and generate the 70 aa-long polypeptide CopA(Z), which helps cells survive toxic copper concentrations. The high efficiency of frameshifting is achieved by the combined stimulatory action of a "slippery" sequence, an mRNA pseudoknot
    Title: Programmed Ribosomal Frameshifting Generates a Copper Transporter and a Copper Chaperone from the Same Gene.
  2. The distal N-terminal metal-binding domain transfers copper to the membrane-integral ion-binding sites of CopA, while the proximal metal-binding domain has a regulatory role by suppressing the catalytic activity of CopA in absence of copper.
    Title: Distinct functions of serial metal-binding domains in the Escherichia coli P1 B -ATPase CopA.
  3. Data indicate that RNAP sigma(70)-can bind to copper efflux regulator (CueR)-promoter PcopA complex.
    Title: Metalloregulator CueR biases RNA polymerase's kinetic sampling of dead-end or open complex to repress or activate transcription.
  4. copper-transporting ATPases, CopA and ATP7A, in both bacteria and macrophage are unique determinants of bacteria survival and identify an unexpected role for copper at the host-pathogen interface
    Title: A role for the ATP7A copper-transporting ATPase in macrophage bactericidal activity.
  5. N-terminus verified by Edman degradation on mature peptide
    Title: Small genes/gene-products in Escherichia coli K-12.
Submit: New GeneRIF Correction

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables P-type ion transporter activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables P-type monovalent copper transporter activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables copper ion binding IBA
Inferred from Biological aspect of Ancestor
more info
  
enables silver ion transmembrane transporter activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Process Evidence Code Pubs
acts_upstream_of_or_within cellular response to copper ion IEP
Inferred from Expression Pattern
more info
 PubMed 
acts_upstream_of_or_within cellular response to silver ion IEP
Inferred from Expression Pattern
more info
 PubMed 
acts_upstream_of_or_within copper ion export EXP
Inferred from Experiment
more info
 PubMed 
acts_upstream_of_or_within copper ion export IDA
Inferred from Direct Assay
more info
 PubMed 
acts_upstream_of_or_within copper ion export IEP
Inferred from Expression Pattern
more info
 PubMed 
acts_upstream_of_or_within copper ion export IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in copper ion homeostasis IBA
Inferred from Biological aspect of Ancestor
more info
  
acts_upstream_of_or_within silver ion transmembrane transport IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
is_active_in membrane IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in plasma membrane IDA
Inferred from Direct Assay
more info
 PubMed 
located_in plasma membrane ISM
Inferred from Sequence Model
more info
 PubMed 
Preferred Names
Cu(+) exporting P-type ATPase;soluble Cu(+) chaperone

NEW Try the new Transcript table

Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    508875..511379 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_415017.1 Cu(+) exporting P-type ATPase

    See identical proteins and their annotated locations for NP_415017.1

    Status: REVIEWED

    UniProtKB/TrEMBL
    A0A6M9WTC3
    Conserved Domains (1) summary
    PRK10671
    Location:1 → 834
    copA; copper-exporting P-type ATPase CopA

  2. YP_009518752.1 soluble Cu(+) chaperone

    Status: REVIEWED

    UniProtKB/TrEMBL
    A0A6D0ICQ1
    Conserved Domains (1) summary
    cl27747
    Location:1 → 69
    E1-E2_ATPase; E1-E2 ATPase
Nucleotide Protein
Heading Accession and Version

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.