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Entry version 178 (17 Jun 2020)
Sequence version 4 (23 Jan 2007)
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Protein

Copper-exporting P-type ATPase

Gene

copA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Exports Cu+ from the cytoplasm to the periplasm (PubMed:10639134, PubMed:11167016, PubMed:11500054, PubMed:12351646). Binds 2 Cu+ ions per monomer, which are transferred to periplasmic copper chaperone CusF upon ATP hydrolysis (PubMed:24917681). In vitro an excess of CusF over CopA is required for efficient transfer (PubMed:24917681). May also be involved in silver export (PubMed:12351646, PubMed:12832075).6 Publications
mRNA is subject to programmed ribosomal frameshifting which produces a cytoplasmic copper chaperone CopA(Z) that corresponds to the first HMA domain (PubMed:28107647). The soluble form is essential for cell survivial in the presence of CuSO4; in growth competition experiments between wild-type and a version that prevents expression of CopA(Z) after 50 generations the non-CopA(Z) version is nearly extinct (PubMed:28107647). The first HMA domain (residues 1-70) can be replaced by B.subtilis Cu chaperone CopZ (PubMed:25899340).2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Export is inhibited by vanadate (PubMed:10639134). Phosphorylation is inhibited by vanadate and sensitive to KOH and hydroxylamine; it is not inhibited by azide (PubMed:12351646). Phosphorylation is Cu+ not Cu2+-dependent (PubMed:12351646). ATPase activity is inhibited by bathocuproindisulfonate (BCDS), which chelates Cu+ but not Cu2+, and stimulated 3-4-fold by Cu+ (PubMed:12351646, PubMed:25899340). ATPase activity is inhibited by Cu2+ plus DTT or Ag+ (PubMed:12351646).3 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Export tested with Isoform Copper-exporting P-type ATPase.Curated
  1. KM=1.5 µM for copper1 Publication
  2. KM=0.5 mM for ATP1 Publication
  3. KM=1.48 µM for Cu+1 Publication
  4. KM=5.4 µM for Cu+1 Publication
  1. Vmax=0.19 µmol/min/mg enzyme (in the presence of CuCl2 and 1 mM DTT)1 Publication
  2. Vmax=1.64 µmol/h/mg enzyme for Cu+1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi14CopperPROSITE-ProRule annotation1
Metal bindingi17CopperPROSITE-ProRule annotation1
Metal bindingi110CopperPROSITE-ProRule annotation1
Metal bindingi113CopperPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei5234-aspartylphosphate intermediate1 Publication1
Metal bindingi720MagnesiumPROSITE-ProRule annotation1
Metal bindingi724MagnesiumPROSITE-ProRule annotation1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionChaperone, Translocase
Biological processCopper transport, Ion transport, Transport
LigandATP-binding, Copper, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
ECOL316407:JW0473-MONOMER
MetaCyc:G6260-MONOMER

SABIO-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
Q59385

Protein family/group databases

Transport Classification Database

More...
TCDBi
3.A.3.5.5 the p-type atpase (p-atpase) superfamily

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Copper-exporting P-type ATPase1 Publication (EC:7.2.2.82 Publications)
Alternative name(s):
Copper-exporting P-type ATPase A
Cu(+)-exporting ATPase
Soluble copper chaperone CopA(Z)1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:copA1 Publication
Synonyms:atcU1 Publication, f834, ybaR
Ordered Locus Names:b0484, JW0473
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini2 – 186CytoplasmicCuratedAdd BLAST185
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei187 – 207HelicalSequence analysisAdd BLAST21
Topological domaini208 – 217Periplasmic; loop 11 Publication10
Transmembranei218 – 238HelicalSequence analysisAdd BLAST21
Topological domaini239 – 253CytoplasmicCuratedAdd BLAST15
Transmembranei254 – 274HelicalSequence analysisAdd BLAST21
Topological domaini275 – 283Periplasmic; loop 21 Publication9
Transmembranei284 – 304HelicalSequence analysisAdd BLAST21
Topological domaini305 – 437CytoplasmicCuratedAdd BLAST133
Transmembranei438 – 458HelicalSequence analysisAdd BLAST21
Topological domaini459 – 463Periplasmic; loop 3Curated5
Transmembranei464 – 484HelicalSequence analysisAdd BLAST21
Topological domaini485 – 778CytoplasmicCuratedAdd BLAST294
Transmembranei779 – 799HelicalSequence analysisAdd BLAST21
Topological domaini800Periplasmic; loop 41 Publication1
Transmembranei801 – 821HelicalSequence analysisAdd BLAST21
Topological domaini822 – 834Cytoplasmic1 PublicationAdd BLAST13

GO - Cellular componenti

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Cytoplasm, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Decreased resistance to Cu+ (PubMed:10639134, PubMed:11167016). No change in resistance to Zn2+ or Cd2+ (PubMed:10639134). Decreased resistance to AgNO3 (PubMed:12832075). Increased intracellular levels of Cu2+ (PubMed:11167016).3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi1 – 70Missing : Slight increase in CuSO(4)-stimulation of ATPase, no growth in CuSO(4). Grows when this protein fragment is provided in trans or if B.subtilis CopZ is present. 1 PublicationAdd BLAST70
Mutagenesisi3 – 113Missing : No resistance to CuSO(4), does not form phosphate intermediate. 1 PublicationAdd BLAST111
Mutagenesisi7 – 54Missing : Partial resistance to CuSO(4), forms phosphate intermediate. 1 PublicationAdd BLAST48
Mutagenesisi8 – 150Missing : Loss of growth in the presence of CuSO(4), loss of Cu efflux. 1 PublicationAdd BLAST143
Mutagenesisi14 – 17CGHC → AGHA: Wild-type growth in the presence of CuSO(4), no change in Cu efflux. Still forms phosphate intermediate; when associated with 110-A--A-113. 2 Publications4
Mutagenesisi14 – 17CGHC → SGHS: No change in CuSO(4)-stimulation of ATPase. When expressed as an isolated protein fragment (residues 1-70) does not restore growth to the 71-K--G-834 fragment. 1 Publication4
Mutagenesisi32 – 67EQADV…ASVSH → SRRMCLSLKRTLPGLPVQNS RSKPSNKRVMTHLYAN: Reduces -1 frameshifting efficiency about 2-fold in a 104 residue truncated construct. 1 PublicationAdd BLAST36
Mutagenesisi110 – 113CASC → AASA: Wild-type growth in the presence of CuSO(4), no change in Cu efflux. Still forms phosphate intermediate; when associated with 14-A--A-17. 2 Publications4
Mutagenesisi110 – 113CASC → SASS: Loss of CuSO(4)-stimulation of ATPase. When present in the 51-K--G-834 fragment growth in CuSO(4) is not restored by protein fragment 1-M--A-70. 1 Publication4
Mutagenesisi204M → A: Decreased transfer of Cu(+) to CusF, binds 2 Cu(+). 1 Publication1
Mutagenesisi207 – 210DNMM → AAAA: First half of periplasmic loop 1, transfers about 10% Cu(+) to CusF. 1 Publication4
Mutagenesisi212 – 216TADNR → AAANA: Second half of periplasmic loop 1, wild-type transfer of Cu(+) to CusF. 1 Publication5
Mutagenesisi273 – 277WPQWF → APQAA: First half of periplasmic loop 2, nearly wild-type transfer of Cu(+) to CusF. 1 Publication5
Mutagenesisi279 – 283MEARH → AAARA: Second half of periplasmic loop 2, wild-type transfer of Cu(+) to CusF. 1 Publication5
Mutagenesisi287E → A: Decreased transfer of Cu(+) to CusF. 1 Publication1
Mutagenesisi479C → A: Loss of copper resistance, transport and phosphoenzyme formation. 1 Publication1
Mutagenesisi481C → A or H: Loss of copper resistance, transport and phosphoenzyme formation. 1 Publication1
Mutagenesisi797 – 802WPFTGT → APFAGA: Periplasmic loop 4, nearly wild-type transfer of Cu(+) to CusF. 1 Publication6

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000463202 – 834Copper-exporting P-type ATPaseAdd BLAST833

Keywords - PTMi

Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q59385

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q59385

PRoteomics IDEntifications database

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PRIDEi
Q59385

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Induced by Cu2+ and Ag+ (at protein level) (PubMed:10639134). Transcriptionally regulated by CueR in response to Cu+ or Ag+ ions (PubMed:10639134, PubMed:11167016). Basal expression is low but unperturbed by disruption of cueR (PubMed:11167016).2 Publications

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Copper-exporting P-type ATPase interacts with apo-periplasmic copper chaperone CusF; when CusF is precharged with copper it binds very little CopA. The periplasmic loops of CopA, especially the first half of loop 1, play a large role in binding to CusF (PubMed:24917681).

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
4261336, 115 interactors

Protein interaction database and analysis system

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IntActi
Q59385, 6 interactors

STRING: functional protein association networks

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STRINGi
511145.b0484

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q59385

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini4 – 65HMA 1PROSITE-ProRule annotationAdd BLAST62
Domaini100 – 163HMA 2PROSITE-ProRule annotationAdd BLAST64

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi14 – 17CXXC motif 11 Publication4
Motifi110 – 113CXXC motif 21 Publication4

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The N-terminal domain (exact residues are not given in the paper) is not required for Cu+-binding (when deleted KM for Cu+ binding is 1.32 µM) nor for ATPase activity, binds 2 Cu+/monomer (PubMed:24917681). Contradictory results give a considerable decrease in Cu affinity when residues 1-150 are deleted (KM=31.9 µM for Cu+) (PubMed:25899340). The first of 2 N-terminal heavy metal-binding domains (HMA 1, approximately residues 1-70, equivalent to CopA(Z)) has a 5-fold higher affinity for Cu+ than HMA 2 (residues 71-150) and as a protein fragment can transfer Cu+ to the ATPase fragment (residues 151-834), suggesting it has a Cu-chaperone function (PubMed:25899340). HMA 2 transfers Cu+ to HMA 1 but the opposite reaction does not occur in vitro (PubMed:25899340). The HMA 1 fragment complements growth defects in trans, but if its CXXC motif is mutated, or if the remaining CXXC motif in HMA2 is mutated, complementation no longer occurs, showing the 2 HMA domains have different functions (PubMed:25899340). The periplasmic loops of CopA, especially the first half of loop 1, play a large role in binding to CusF (PubMed:24917681). Contradictory results between the various in vitro studies may be due to different levels of protein expression or reconstitution (Probable).Curated2 Publications

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105C59 Bacteria
COG2217 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_001771_0_3_6

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q59385

KEGG Orthology (KO)

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KOi
K17686

Database for complete collections of gene phylogenies

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PhylomeDBi
Q59385

Family and domain databases

Conserved Domains Database

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CDDi
cd00371 HMA, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.40.1110.10, 1 hit
3.40.50.1000, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR023299 ATPase_P-typ_cyto_dom_N
IPR018303 ATPase_P-typ_P_site
IPR023298 ATPase_P-typ_TM_dom_sf
IPR008250 ATPase_P-typ_transduc_dom_A_sf
IPR036412 HAD-like_sf
IPR023214 HAD_sf
IPR017969 Heavy-metal-associated_CS
IPR006121 HMA_dom
IPR036163 HMA_dom_sf
IPR027256 P-typ_ATPase_IB
IPR001757 P_typ_ATPase

Pfam protein domain database

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Pfami
View protein in Pfam
PF00403 HMA, 2 hits

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00120 HATPASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF55008 SSF55008, 2 hits
SSF56784 SSF56784, 1 hit
SSF81653 SSF81653, 1 hit
SSF81665 SSF81665, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01525 ATPase-IB_hvy, 1 hit
TIGR01494 ATPase_P-type, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00154 ATPASE_E1_E2, 1 hit
PS01047 HMA_1, 1 hit
PS50846 HMA_2, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by ribosomal frameshifting. AlignAdd to basket
Isoform Copper-exporting P-type ATPase (identifier: Q59385-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MSQTIDLTLD GLSCGHCVKR VKESLEQRPD VEQADVSITE AHVTGTASAE
60 70 80 90 100
QLIETIKQAG YDASVSHPKA KPLAESSIPS EALTAVSEAL PAATADDDDS
110 120 130 140 150
QQLLLSGMSC ASCVTRVQNA LQSVPGVTQA RVNLAERTAL VMGSASPQDL
160 170 180 190 200
VQAVEKAGYG AEAIEDDAKR RERQQETAVA TMKRFRWQAI VALAVGIPVM
210 220 230 240 250
VWGMIGDNMM VTADNRSLWL VIGLITLAVM VFAGGHFYRS AWKSLLNGAA
260 270 280 290 300
TMDTLVALGT GVAWLYSMSV NLWPQWFPME ARHLYYEASA MIIGLINLGH
310 320 330 340 350
MLEARARQRS SKALEKLLDL TPPTARLVTD EGEKSVPLAE VQPGMLLRLT
360 370 380 390 400
TGDRVPVDGE ITQGEAWLDE AMLTGEPIPQ QKGEGDSVHA GTVVQDGSVL
410 420 430 440 450
FRASAVGSHT TLSRIIRMVR QAQSSKPEIG QLADKISAVF VPVVVVIALV
460 470 480 490 500
SAAIWYFFGP APQIVYTLVI ATTVLIIACP CALGLATPMS IISGVGRAAE
510 520 530 540 550
FGVLVRDADA LQRASTLDTV VFDKTGTLTE GKPQVVAVKT FADVDEAQAL
560 570 580 590 600
RLAAALEQGS SHPLARAILD KAGDMQLPQV NGFRTLRGLG VSGEAEGHAL
610 620 630 640 650
LLGNQALLNE QQVGTKAIEA EITAQASQGA TPVLLAVDGK AVALLAVRDP
660 670 680 690 700
LRSDSVAALQ RLHKAGYRLV MLTGDNPTTA NAIAKEAGID EVIAGVLPDG
710 720 730 740 750
KAEAIKHLQS EGRQVAMVGD GINDAPALAQ ADVGIAMGGG SDVAIETAAI
760 770 780 790 800
TLMRHSLMGV ADALAISRAT LHNMKQNLLG AFIYNSIGIP VAAGILWPFT
810 820 830
GTLLNPVVAG AAMALSSITV VSNANRLLRF KPKE
Length:834
Mass (Da):87,873
Last modified:January 23, 2007 - v4
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iCF84A18FE208E6F6
GO
Isoform Soluble copper chaperone CopA(Z) (identifier: Q59385-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     70-834: AKPLAESSIP...NRLLRFKPKE → G

Note: Expression of the CopA(Z) soluble copper chaperone isoform requires a -1 programmed ribosomal frameshift (PRF) at the 70th codon, promoted by a nucleotide 'slippery sequence'. Silent mutations in the 'slippery sequence' abrogate expression of CopA(Z) but still allow expression of the full length protein. Both the mRNA secondary structure (a possible pseudoknot just downstream of the slippage site) and the sequence of the protein in the ribosomal exit tunnel modulate the efficiency of the -1 PRF (PubMed:28107647).1 Publication
Show »
Length:70
Mass (Da):7,481
Checksum:iF0370BB67BCFDC7A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti162 – 181EAIED…TAVAT → KRLKMTLNAASASKKPPSLA in AAB02268 (Ref. 1) CuratedAdd BLAST20
Sequence conflicti508A → R in AAB02268 (Ref. 1) Curated1
Sequence conflicti576Q → R in AAB02268 (Ref. 1) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_05917670 – 834AKPLA…FKPKE → G in isoform Soluble copper chaperone CopA(Z). 1 PublicationAdd BLAST765

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U58330 Genomic DNA Translation: AAB02268.1
U82664 Genomic DNA Translation: AAB40238.1
U00096 Genomic DNA Translation: AAC73586.1
U00096 Genomic DNA Translation: AYC08180.1
AP009048 Genomic DNA Translation: BAE76263.1

Protein sequence database of the Protein Information Resource

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PIRi
C64779

NCBI Reference Sequences

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RefSeqi
NP_415017.1, NC_000913.3
WP_000083955.1, NZ_SSZK01000009.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73586; AAC73586; b0484
BAE76263; BAE76263; BAE76263

Database of genes from NCBI RefSeq genomes

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GeneIDi
946106

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0473
eco:b0484

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.1792

Keywords - Coding sequence diversityi

Ribosomal frameshifting

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58330 Genomic DNA Translation: AAB02268.1
U82664 Genomic DNA Translation: AAB40238.1
U00096 Genomic DNA Translation: AAC73586.1
U00096 Genomic DNA Translation: AYC08180.1
AP009048 Genomic DNA Translation: BAE76263.1
PIRiC64779
RefSeqiNP_415017.1, NC_000913.3
WP_000083955.1, NZ_SSZK01000009.1

3D structure databases

SMRiQ59385
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi4261336, 115 interactors
IntActiQ59385, 6 interactors
STRINGi511145.b0484

Protein family/group databases

TCDBi3.A.3.5.5 the p-type atpase (p-atpase) superfamily

Proteomic databases

jPOSTiQ59385
PaxDbiQ59385
PRIDEiQ59385

Genome annotation databases

EnsemblBacteriaiAAC73586; AAC73586; b0484
BAE76263; BAE76263; BAE76263
GeneIDi946106
KEGGiecj:JW0473
eco:b0484
PATRICifig|1411691.4.peg.1792

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB3035

Phylogenomic databases

eggNOGiENOG4105C59 Bacteria
COG2217 LUCA
HOGENOMiCLU_001771_0_3_6
InParanoidiQ59385
KOiK17686
PhylomeDBiQ59385

Enzyme and pathway databases

BioCyciECOL316407:JW0473-MONOMER
MetaCyc:G6260-MONOMER
SABIO-RKiQ59385

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q59385

Family and domain databases

CDDicd00371 HMA, 2 hits
Gene3Di3.40.1110.10, 1 hit
3.40.50.1000, 1 hit
InterProiView protein in InterPro
IPR023299 ATPase_P-typ_cyto_dom_N
IPR018303 ATPase_P-typ_P_site
IPR023298 ATPase_P-typ_TM_dom_sf
IPR008250 ATPase_P-typ_transduc_dom_A_sf
IPR036412 HAD-like_sf
IPR023214 HAD_sf
IPR017969 Heavy-metal-associated_CS
IPR006121 HMA_dom
IPR036163 HMA_dom_sf
IPR027256 P-typ_ATPase_IB
IPR001757 P_typ_ATPase
PfamiView protein in Pfam
PF00403 HMA, 2 hits
PRINTSiPR00120 HATPASE
SUPFAMiSSF55008 SSF55008, 2 hits
SSF56784 SSF56784, 1 hit
SSF81653 SSF81653, 1 hit
SSF81665 SSF81665, 1 hit
TIGRFAMsiTIGR01525 ATPase-IB_hvy, 1 hit
TIGR01494 ATPase_P-type, 1 hit
PROSITEiView protein in PROSITE
PS00154 ATPASE_E1_E2, 1 hit
PS01047 HMA_1, 1 hit
PS50846 HMA_2, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCOPA_ECOLI
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q59385
Secondary accession number(s): A0A385XJA3, P78245, Q2MBU3
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: June 17, 2020
This is version 178 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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