O29777 · COPA_ARCFU

Function

function

Probably involved in copper and silver export.

Catalytic activity

Activity regulation

Activated by Cu+ and Ag+ and inhibited by vanadate. Activated by CopZ in its Cu+-bound form.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
0.25 mMATP
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
14.9 μmol/h/mgwith Ag+ as substrate
3.7 μmol/h/mgwith Cu+ as substrate
Shows higher affinity for Cu+ compared with Ag+.

pH Dependence

Optimum pH is 6.1-6.5.

Temperature Dependence

Optimum temperature is 75 degrees Celsius.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site27Cu+ 1 (UniProtKB | ChEBI)
Binding site30Cu+ 1 (UniProtKB | ChEBI)
Active site4244-aspartylphosphate intermediate
Binding site457-462ATP (UniProtKB | ChEBI)
Binding site490-501ATP (UniProtKB | ChEBI)
Binding site618Mg2+ (UniProtKB | ChEBI)
Binding site622Mg2+ (UniProtKB | ChEBI)
Binding site751Cu+ 2 (UniProtKB | ChEBI)
Binding site754Cu+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentplasma membrane
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular Functioncopper ion binding
Molecular Functionidentical protein binding
Molecular FunctionP-type monovalent copper transporter activity

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Probable copper-exporting P-type ATPase
  • EC number
  • Alternative names
    • Copper-exporting P-type ATPase A
    • Cu(+)-exporting ATPase

Gene names

    • Name
      copA
    • Synonyms
      pacS
    • Ordered locus names
      AF_0473

Organism names

Accessions

  • Primary accession
    O29777

Proteomes

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-101Cytoplasmic
Transmembrane102-122Helical
Topological domain123-128Extracellular
Transmembrane129-149Helical
Topological domain150-159Cytoplasmic
Transmembrane160-180Helical
Topological domain181-186Extracellular
Transmembrane187-204Helical
Topological domain205-339Cytoplasmic
Transmembrane340-360Helical
Topological domain361-364Extracellular
Transmembrane365-385Helical
Topological domain386-680Cytoplasmic
Transmembrane681-701Helical
Topological domain702-704Extracellular
Transmembrane705-725Helical
Topological domain726-804Cytoplasmic

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis27Reduction in ATPase activity; when associated with A-30.
Mutagenesis30Reduction in ATPase activity; when associated with A-27.
Mutagenesis380Abolishes activity.
Mutagenesis382Abolishes activity.
Mutagenesis751No effect on ATPase activity; when associated with A-754. Reduction in ATPase activity; when associated with A-27; A-30 and A-754.
Mutagenesis754No effect on ATPase activity, when associated with A-751. Reduction in ATPase activity; when associated with A-27; A-30 and A-751.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003506011-804Probable copper-exporting P-type ATPase

Keywords

Proteomic databases

Interaction

Subunit

Interacts with CopZ probably in the CopZ Cu+-bound form.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY O29777copA O297772EBI-9016967, EBI-9016967

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain16-82HMA 1
Domain740-801HMA 2

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    804
  • Mass (Da)
    86,432
  • Last updated
    1998-01-01 v1
  • Checksum
    610EB948C1D6B16F
MVKDTYISSASKTPPMERTVRVTGMTCAMCVKSIETAVGSLEGVEEVRVNLATETAFIRFDEKRIDFETIKRVIEDLGYGVVDEQAAVSAEVEHLSRMKRKLYVAAFAGVLLLFLAHFISLPYEDFVQLLIALPAIFYSGSSIFKAAFSALRRRTLNMDVMYSMGVGAAFLASVLSTAGVLPREYSFYETSVLLLAFLLLGRTLEARAKSRTGEAIKKLVGLQAKTAVVIRDGKEIAVPVEEVAVGDIVIVRPGEKIPVDGVVVEGESYVDESMISGEPVPVLKSKGDEVFGATINNTGVLKIRATRVGGETLLAQIVKLVEDAMGSKPPIQRLADKVVAYFIPTVLLVAISAFIYWYFIAHAPLLFAFTTLIAVLVVACPCAFGLATPTALTVGMGKGAELGILIKNADALEVAEKVTAVIFDKTGTLTKGKPEVTDLVPLNGDERELLRLAAIAERRSEHPIAEAIVKKALEHGIELGEPEKVEVIAGEGVVADGILVGNKRLMEDFGVAVSNEVELALEKLEREAKTAVIVARNGRVEGIIAVSDTLKESAKPAVQELKRMGIKVGMITGDNWRSAEAISRELNLDLVIAEVLPHQKSEEVKKLQAKEVVAFVGDGINDAPALAQADLGIAVGSGSDVAVESGDIVLIRDDLRDVVAAIQLSRKTMSKIKQNIFWALIYNVILIPAAAGLLYPIFGVVFRPEFAGLAMAMSSVSVVANSLLLRNYVPPIRRGGDSVEKIVLELSGLSCHHCVARVKKALEEAGAKVEKVDLNEAVVAGNKEDVDKYIKAVEAAGYQAKLRS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE000782
EMBL· GenBank· DDBJ
AAB90763.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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