UniProt functional annotation for P36655



	UniProt functional annotation for P36655

UniProt code: P36655.

Organism: Escherichia coli (strain K12).

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

Function: Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm, thereby maintaining the active site of DsbC, DsbE and DsbG in a reduced state. This transfer involves a cascade of disulfide bond formation and reduction steps.

Catalytic activity: Reaction=[protein]-dithiol + NAD(+) = [protein]-disulfide + H(+) + NADH; Xref=Rhea:RHEA:18749, Rhea:RHEA-COMP:10593, Rhea:RHEA- COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.8.1.8;

Catalytic activity: Reaction=[protein]-dithiol + NADP(+) = [protein]-disulfide + H(+) + NADPH; Xref=Rhea:RHEA:18753, Rhea:RHEA-COMP:10593, Rhea:RHEA- COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.8;

Subcellular location: Cell inner membrane; Multi-pass membrane protein.

Miscellaneous: The consequences of replacement of the cysteines with alanines were found to depend on the conditions tested and on the reporter system used for the analysis, and then differ depending on the references.

Similarity: Belongs to the thioredoxin family. DsbD subfamily. {ECO:0000305}.

Sequence caution: Sequence=CAA54781.1; Type=Erroneous initiation; Evidence={ECO:0000305}; Sequence=CAA85375.1; Type=Erroneous initiation; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


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



Function:		Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm, thereby maintaining the active site of DsbC, DsbE and DsbG in a reduced state. This transfer involves a cascade of disulfide bond formation and reduction steps.


Catalytic activity:		Reaction=[protein]-dithiol + NAD(+) = [protein]-disulfide + H(+) + NADH; Xref=Rhea:RHEA:18749, Rhea:RHEA-COMP:10593, Rhea:RHEA- COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.8.1.8;
Catalytic activity:		Reaction=[protein]-dithiol + NADP(+) = [protein]-disulfide + H(+) + NADPH; Xref=Rhea:RHEA:18753, Rhea:RHEA-COMP:10593, Rhea:RHEA- COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.8;
Subcellular location:		Cell inner membrane; Multi-pass membrane protein.
Miscellaneous:		The consequences of replacement of the cysteines with alanines were found to depend on the conditions tested and on the reporter system used for the analysis, and then differ depending on the references.
Similarity:		Belongs to the thioredoxin family. DsbD subfamily. {ECO:0000305}.
Sequence caution:		Sequence=CAA54781.1; Type=Erroneous initiation; Evidence={ECO:0000305}; Sequence=CAA85375.1; Type=Erroneous initiation; Evidence={ECO:0000305};