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Information on EC 7.2.2.8 - P-type Cu+ transporter and Organism(s) Bacillus subtilis and UniProt Accession O32220

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EC Tree
IUBMB Comments
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme transports Cu+ or Ag+, and cannot transport the divalent ions, contrary to EC 7.2.2.9, P-type Cu2+ transporter, which mainly transports the divalent copper ion.
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Bacillus subtilis
UNIPROT: O32220
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The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
slc31a1, copt1, ctra2, cu(+)-atpase, copa1, copa2, copper-transporting atpase 2, ctra3, cu atpase, copper export atpase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu(I)-detoxifying P-type ATPase
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Cu(I)-transporting P-type ATPase
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Cu+-exporting ATPase
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-
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (P-type, Cu+-exporting)
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme transports Cu+ or Ag+, and cannot transport the divalent ions, contrary to EC 7.2.2.9, P-type Cu2+ transporter, which mainly transports the divalent copper ion.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O + Cu+[side 1]
ADP + phosphate + Cu+[side 2]
show the reaction diagram
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-
-
?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O + Cu+[side 1]
ADP + phosphate + Cu+[side 2]
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the P-type ATPase CopA plays a major role in the resistance of the cell to copper. The N-terminal domains of Cu(I)-transporting P-type ATPases interact with other domains of the transporter, thereby regulating transport activity
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 8256.44, recombinant N-terminal domain CopAb, mass spectrometry, x * 8258.17, N-terminal domain CopAb, sequence calculation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure determination of the 73-147 domain in the 1-151 construct, in the apo state through 1H, 15N and 13C NMR spectroscopies, the structure of the Cu(I)-loaded 73-147 domain has been also determined in the construct 73-151
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene copAab, recombinant full-length enzyme and N-terminal domains CopAa and CopAb from Escherichia coli strain BL21(DE3) by anion exchange chromatography, ultrafiltration, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene copAab, expression of full-length enzyme and N-terminal domains CopAa and CopAb in Escherichia coli strain BL21(DE3)
the N-terminal region of BsCopA contains two domains constituted by amino acid residues 1 to 72 and 73 to 147, which are expressed both separately and together, in both cases only the 73-147 domain is folded and is stable both in the copper(I)-free and in the copper(I)-bound forms
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Banci, L.; Bertini, I.; Ciofi-Baffoni, S.; D'Onofrio, M.; Gonnelli, L.; Marhuenda-Egea, F.C.; Ruiz-Duenas, F.J.
Solution structure of the N-terminal domain of a potential copper-translocating P-type ATPase from Bacillus subtilis in the apo and Cu(I) loaded states
J. Mol. Biol.
317
415-429
2002
Bacillus subtilis (O32220), Bacillus subtilis
Manually annotated by BRENDA team
Zhou, L.; Singleton, C.; Le Brun, N.E.
CopAb, the second N-terminal soluble domain of Bacillus subtilis CopA, dominates the Cu(I)-binding properties of CopAab
Dalton Trans.
41
5939-5948
2012
Bacillus subtilis (O32220), Bacillus subtilis, Bacillus subtilis 168 (O32220)
Manually annotated by BRENDA team