EC Number | Cloned (Comment) | Organism |
---|---|---|
7.2.2.8 | gene copAab, expression of full-length enzyme and N-terminal domains CopAa and CopAb in Escherichia coli strain BL21(DE3) | Bacillus subtilis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
7.2.2.8 | ATP + H2O + Cu+[side 1] | Bacillus subtilis | - |
ADP + phosphate + Cu+[side 2] | - |
? | |
7.2.2.8 | ATP + H2O + Cu+[side 1] | Bacillus subtilis 168 | - |
ADP + phosphate + Cu+[side 2] | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
7.2.2.8 | Bacillus subtilis | O32220 | - |
- |
7.2.2.8 | Bacillus subtilis 168 | O32220 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
7.2.2.8 | 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 | Bacillus subtilis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
7.2.2.8 | ATP + H2O + Cu+[side 1] | - |
Bacillus subtilis | ADP + phosphate + Cu+[side 2] | - |
? | |
7.2.2.8 | ATP + H2O + Cu+[side 1] | - |
Bacillus subtilis 168 | ADP + phosphate + Cu+[side 2] | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
7.2.2.8 | ? | x * 8256.44, recombinant N-terminal domain CopAb, mass spectrometry, x * 8258.17, N-terminal domain CopAb, sequence calculation | Bacillus subtilis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
7.2.2.8 | CopA | - |
Bacillus subtilis |
7.2.2.8 | Cu(I)-detoxifying P-type ATPase | - |
Bacillus subtilis |
7.2.2.8 | Cu(I)-transporting P-type ATPase | - |
Bacillus subtilis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
7.2.2.8 | additional information | the enzyme CopA contains two N-terminal soluble domains, CopAa and CopAb, connected by a short linker, both domains are able to bind Cu(I) extremely tightly. Isolated N-terminal soluble domains CopAa and CopAb bind Cu(I) with an extremely high affinity and remain as a monomers up to a level of 1 Cu(I) per protein. Above this level, they undergo dimerization. The Cu(I)-binding properties of CopAb are very similar to those of the two-domain protein CopAab, indicating that this domain plays a dominant role in determining the binding properties of CopAab. The MTCAAC Cu(I)-binding motif of each domain is located at opposite ends of the protein molecule, ruling out the possibility of intra protein, inter-domain Cu(I)-binding, proposed model of Cu(I)-binding to CopAb and the resulting association state changes, overview. CopAb in isolation does not undergo Cu(I)-mediated unfolding, the unfolding of CopAab at high levels of Cu(I) is due to the instability of the CopAa domain and the remaining secondary structure observed at high Cu(I) levels in CopAab is due to the stable CopAb domain | Bacillus subtilis |
7.2.2.8 | 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 | Bacillus subtilis |