UniProt functional annotation for P36649



	UniProt functional annotation for P36649

UniProt code: P36649.

Organism: Escherichia coli (strain K12).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.

Function: Probably involved in periplasmic detoxification of copper by oxidizing Cu(+) to Cu(2+) and thus preventing its uptake into the cytoplasm. Possesses phenoloxidase and ferroxidase activities and might be involved in the production of polyphenolic compounds and the prevention of oxidative damage in the periplasm.

Cofactor: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Note=Binds 4 Cu cations per monomer.;

Subunit: Monomer. {ECO:0000305}.

Subcellular location: Periplasm. Note=It is exported via the Tat pathway.

Induction: By CueR, at increased levels of cytoplasmic cuprous ions.

Domain: The methionine-rich domain could provide binding sites for exogenous copper ions. This methionine-rich region is probably important for copper tolerance in bacteria.

Ptm: Exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven. Can also be exported by the Sec system.

Miscellaneous: This protein is sensitive to oxygen deprivation. It probably plays a significant role in copper efflux under aerobic conditions.

Similarity: Belongs to the multicopper oxidase family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia coli (strain K12).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.



Function:		Probably involved in periplasmic detoxification of copper by oxidizing Cu(+) to Cu(2+) and thus preventing its uptake into the cytoplasm. Possesses phenoloxidase and ferroxidase activities and might be involved in the production of polyphenolic compounds and the prevention of oxidative damage in the periplasm.


Cofactor:		Name=Cu cation; Xref=ChEBI:CHEBI:23378; Note=Binds 4 Cu cations per monomer.;
Subunit:		Monomer. {ECO:0000305}.
Subcellular location:		Periplasm. Note=It is exported via the Tat pathway.
Induction:		By CueR, at increased levels of cytoplasmic cuprous ions.
Domain:		The methionine-rich domain could provide binding sites for exogenous copper ions. This methionine-rich region is probably important for copper tolerance in bacteria.
Ptm:		Exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven. Can also be exported by the Sec system.
Miscellaneous:		This protein is sensitive to oxygen deprivation. It probably plays a significant role in copper efflux under aerobic conditions.
Similarity:		Belongs to the multicopper oxidase family. {ECO:0000305}.