O29777 · COPA_ARCFU
- ProteinProbable copper-exporting P-type ATPase
- GenecopA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids804 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Probably involved in copper and silver export.
Catalytic activity
- ATP + Cu+(in) + H2O = ADP + Cu+(out) + H+ + phosphate
CHEBI:30616 + Cu+ (in)CHEBI:49552+ CHEBI:15377 = CHEBI:456216 + Cu+ (out)CHEBI:49552+ CHEBI:15378 + CHEBI:43474
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 mM | ATP |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
14.9 μmol/h/mg | with Ag+ as substrate | ||||
3.7 μmol/h/mg | with 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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 27 | Cu+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 30 | Cu+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Active site | 424 | 4-aspartylphosphate intermediate | ||||
Sequence: D | ||||||
Binding site | 457-462 | ATP (UniProtKB | ChEBI) | ||||
Sequence: ERRSEH | ||||||
Binding site | 490-501 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GEGVVADGILVG | ||||||
Binding site | 618 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 622 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 751 | Cu+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 754 | Cu+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | copper ion binding | |
Molecular Function | identical protein binding | |
Molecular Function | P-type monovalent copper transporter activity |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameProbable copper-exporting P-type ATPase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Archaeoglobi > Archaeoglobales > Archaeoglobaceae > Archaeoglobus
Accessions
- Primary accessionO29777
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-101 | Cytoplasmic | ||||
Sequence: MVKDTYISSASKTPPMERTVRVTGMTCAMCVKSIETAVGSLEGVEEVRVNLATETAFIRFDEKRIDFETIKRVIEDLGYGVVDEQAAVSAEVEHLSRMKRK | ||||||
Transmembrane | 102-122 | Helical | ||||
Sequence: LYVAAFAGVLLLFLAHFISLP | ||||||
Topological domain | 123-128 | Extracellular | ||||
Sequence: YEDFVQ | ||||||
Transmembrane | 129-149 | Helical | ||||
Sequence: LLIALPAIFYSGSSIFKAAFS | ||||||
Topological domain | 150-159 | Cytoplasmic | ||||
Sequence: ALRRRTLNMD | ||||||
Transmembrane | 160-180 | Helical | ||||
Sequence: VMYSMGVGAAFLASVLSTAGV | ||||||
Topological domain | 181-186 | Extracellular | ||||
Sequence: LPREYS | ||||||
Transmembrane | 187-204 | Helical | ||||
Sequence: FYETSVLLLAFLLLGRTL | ||||||
Topological domain | 205-339 | Cytoplasmic | ||||
Sequence: EARAKSRTGEAIKKLVGLQAKTAVVIRDGKEIAVPVEEVAVGDIVIVRPGEKIPVDGVVVEGESYVDESMISGEPVPVLKSKGDEVFGATINNTGVLKIRATRVGGETLLAQIVKLVEDAMGSKPPIQRLADKVV | ||||||
Transmembrane | 340-360 | Helical | ||||
Sequence: AYFIPTVLLVAISAFIYWYFI | ||||||
Topological domain | 361-364 | Extracellular | ||||
Sequence: AHAP | ||||||
Transmembrane | 365-385 | Helical | ||||
Sequence: LLFAFTTLIAVLVVACPCAFG | ||||||
Topological domain | 386-680 | Cytoplasmic | ||||
Sequence: LATPTALTVGMGKGAELGILIKNADALEVAEKVTAVIFDKTGTLTKGKPEVTDLVPLNGDERELLRLAAIAERRSEHPIAEAIVKKALEHGIELGEPEKVEVIAGEGVVADGILVGNKRLMEDFGVAVSNEVELALEKLEREAKTAVIVARNGRVEGIIAVSDTLKESAKPAVQELKRMGIKVGMITGDNWRSAEAISRELNLDLVIAEVLPHQKSEEVKKLQAKEVVAFVGDGINDAPALAQADLGIAVGSGSDVAVESGDIVLIRDDLRDVVAAIQLSRKTMSKIKQNIFWAL | ||||||
Transmembrane | 681-701 | Helical | ||||
Sequence: IYNVILIPAAAGLLYPIFGVV | ||||||
Topological domain | 702-704 | Extracellular | ||||
Sequence: FRP | ||||||
Transmembrane | 705-725 | Helical | ||||
Sequence: EFAGLAMAMSSVSVVANSLLL | ||||||
Topological domain | 726-804 | Cytoplasmic | ||||
Sequence: RNYVPPIRRGGDSVEKIVLELSGLSCHHCVARVKKALEEAGAKVEKVDLNEAVVAGNKEDVDKYIKAVEAAGYQAKLRS |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 27 | Reduction in ATPase activity; when associated with A-30. | ||||
Sequence: C → A | ||||||
Mutagenesis | 30 | Reduction in ATPase activity; when associated with A-27. | ||||
Sequence: C → A | ||||||
Mutagenesis | 380 | Abolishes activity. | ||||
Sequence: C → A | ||||||
Mutagenesis | 382 | Abolishes activity. | ||||
Sequence: C → A or S | ||||||
Mutagenesis | 751 | No effect on ATPase activity; when associated with A-754. Reduction in ATPase activity; when associated with A-27; A-30 and A-754. | ||||
Sequence: C → A | ||||||
Mutagenesis | 754 | No effect on ATPase activity, when associated with A-751. Reduction in ATPase activity; when associated with A-27; A-30 and A-751. | ||||
Sequence: C → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000350601 | 1-804 | Probable copper-exporting P-type ATPase | |||
Sequence: MVKDTYISSASKTPPMERTVRVTGMTCAMCVKSIETAVGSLEGVEEVRVNLATETAFIRFDEKRIDFETIKRVIEDLGYGVVDEQAAVSAEVEHLSRMKRKLYVAAFAGVLLLFLAHFISLPYEDFVQLLIALPAIFYSGSSIFKAAFSALRRRTLNMDVMYSMGVGAAFLASVLSTAGVLPREYSFYETSVLLLAFLLLGRTLEARAKSRTGEAIKKLVGLQAKTAVVIRDGKEIAVPVEEVAVGDIVIVRPGEKIPVDGVVVEGESYVDESMISGEPVPVLKSKGDEVFGATINNTGVLKIRATRVGGETLLAQIVKLVEDAMGSKPPIQRLADKVVAYFIPTVLLVAISAFIYWYFIAHAPLLFAFTTLIAVLVVACPCAFGLATPTALTVGMGKGAELGILIKNADALEVAEKVTAVIFDKTGTLTKGKPEVTDLVPLNGDERELLRLAAIAERRSEHPIAEAIVKKALEHGIELGEPEKVEVIAGEGVVADGILVGNKRLMEDFGVAVSNEVELALEKLEREAKTAVIVARNGRVEGIIAVSDTLKESAKPAVQELKRMGIKVGMITGDNWRSAEAISRELNLDLVIAEVLPHQKSEEVKKLQAKEVVAFVGDGINDAPALAQADLGIAVGSGSDVAVESGDIVLIRDDLRDVVAAIQLSRKTMSKIKQNIFWALIYNVILIPAAAGLLYPIFGVVFRPEFAGLAMAMSSVSVVANSLLLRNYVPPIRRGGDSVEKIVLELSGLSCHHCVARVKKALEEAGAKVEKVDLNEAVVAGNKEDVDKYIKAVEAAGYQAKLRS |
Keywords
- PTM
Proteomic databases
Interaction
Subunit
Interacts with CopZ probably in the CopZ Cu+-bound form.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O29777 | copA O29777 | 2 | EBI-9016967, EBI-9016967 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 16-82 | HMA 1 | ||||
Sequence: MERTVRVTGMTCAMCVKSIETAVGSLEGVEEVRVNLATETAFIRFDEKRIDFETIKRVIEDLGYGVV | ||||||
Domain | 740-801 | HMA 2 | ||||
Sequence: EKIVLELSGLSCHHCVARVKKALEEAGAKVEKVDLNEAVVAGNKEDVDKYIKAVEAAGYQAK |
Sequence similarities
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length804
- Mass (Da)86,432
- Last updated1998-01-01 v1
- Checksum610EB948C1D6B16F
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE000782 EMBL· GenBank· DDBJ | AAB90763.1 EMBL· GenBank· DDBJ | Genomic DNA |