Cytochromes c typically function in electron transfer. They are required during oxidative phosphorylation as an electron shuttle between Complex III (cytochrome c reductase) and IV (cytochrome c oxidase), but c-type cytochrome centers are also found in the active sites of many enzymes; Cytochrome c binds a heme as prosthetic group by Cys85 and Cys88. His89 is involved in iron binding; Belongs to class I (mono-heme) of Cytochrome c; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 16 and 17; Probably localized in the cytoplasmic and/or outer membrane; Funct [...]

Conserved hypothetical membrane protein; Contains four transmembranes segments; Localized in the cytoplasmic membrane; Conserved hypothetical protein.

Cytochromes c typically function in electron transfer. They are required during oxidative phosphorylation as an electron shuttle between Complex III (cytochrome c reductase) and IV (cytochrome c oxidase), but c-type cytochrome centers are also found in the active sites of many enzymes; Cytochrome c binds a heme as prosthetic group by Cys85 and Cys88. His89 is involved in iron binding; Belongs to class I (mono-heme) of Cytochrome c; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 16 and 17; Probably localized in the cytoplasmic and/or outer membrane; Funct [...]

Conserved hypothetical membrane protein; Contains twelve transmembrane segments; Localized in the cytoplasmic membrane; Conserved hypothetical protein.

Cytochromes c typically function in electron transfer. They are required during oxidative phosphorylation as an electron shuttle between Complex III (cytochrome c reductase) and IV (cytochrome c oxidase), but c-type cytochrome centers are also found in the active sites of many enzymes; Cytochrome c binds a heme as prosthetic group by Cys85 and Cys88. His89 is involved in iron binding; Belongs to class I (mono-heme) of Cytochrome c; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 16 and 17; Probably localized in the cytoplasmic and/or outer membrane; Funct [...]

Rieske [2Fe-2S] iron-sulfur protein; Protein that contains an unknown function N-terminal domain and a C-terminal Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines that one Fe ion while the other Fe ion is coordinated by two conserved histidines; Prokaryotic lipoprotein signal peptide cleaved between the residues 25 and 26; Localized in the outer membrane; Function unclear.

Cytochromes c typically function in electron transfer. They are required during oxidative phosphorylation as an electron shuttle between Complex III (cytochrome c reductase) and IV (cytochrome c oxidase), but c-type cytochrome centers are also found in the active sites of many enzymes; Cytochrome c binds a heme as prosthetic group by Cys85 and Cys88. His89 is involved in iron binding; Belongs to class I (mono-heme) of Cytochrome c; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 16 and 17; Probably localized in the cytoplasmic and/or outer membrane; Funct [...]

Fusion of the subunits CcoN and CcoO of the Cytochrome cbb3 oxidase. Converts the ferrocytochrome to ferricytochrome. Belongs to the ccoNOQP operon. Contains 13 transmembrane helices; Localized in the cytoplasmic membrane; High confidence in function and specificity.

Cytochromes c typically function in electron transfer. They are required during oxidative phosphorylation as an electron shuttle between Complex III (cytochrome c reductase) and IV (cytochrome c oxidase), but c-type cytochrome centers are also found in the active sites of many enzymes; Cytochrome c binds a heme as prosthetic group by Cys85 and Cys88. His89 is involved in iron binding; Belongs to class I (mono-heme) of Cytochrome c; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 16 and 17; Probably localized in the cytoplasmic and/or outer membrane; Funct [...]

Molybdopterin oxidoreductase, iron-sulfur binding subunit; Ferredoxins are iron-sulphur proteins that mediate electron transfer in a range of metabolic reactions; Contains 4 4Fe-4S type ferredoxin domains and a putatif Twin-arginine translocation pathway signal; Localized in the cytoplasmic membrane; Family membership.

Cytochromes c typically function in electron transfer. They are required during oxidative phosphorylation as an electron shuttle between Complex III (cytochrome c reductase) and IV (cytochrome c oxidase), but c-type cytochrome centers are also found in the active sites of many enzymes; Cytochrome c binds a heme as prosthetic group by Cys85 and Cys88. His89 is involved in iron binding; Belongs to class I (mono-heme) of Cytochrome c; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 16 and 17; Probably localized in the cytoplasmic and/or outer membrane; Funct [...]

Copper-binding periplasmic protein; Protein which is thought to insert copper into the exported nitrous oxide reductase apoenzyme (NosZ). Belongs to the nitrous oxide reductase operon. Signal peptide cleaved between the residues 22 and 23. Localized in the periplasmic space; High confidence in function and specificity.

Cytochromes c typically function in electron transfer. They are required during oxidative phosphorylation as an electron shuttle between Complex III (cytochrome c reductase) and IV (cytochrome c oxidase), but c-type cytochrome centers are also found in the active sites of many enzymes; Cytochrome c binds a heme as prosthetic group by Cys85 and Cys88. His89 is involved in iron binding; Belongs to class I (mono-heme) of Cytochrome c; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 16 and 17; Probably localized in the cytoplasmic and/or outer membrane; Funct [...]

Copper ABC transporter, ATPase component; This protein, involved in copper processing/transport, is the nucleotide-binding domain of the ABC transporters (ABC ATPase); Responsible for coupling the energy of ATP hydrolysis to conformational changes in the permease component (ABC membrane). Belongs to the nitrous oxide reductase operon. It is a peripheral membrane protein localized near of the cytoplasmic membrane by association with the permease component; High confidence in function and specificity.

Cytochromes c typically function in electron transfer. They are required during oxidative phosphorylation as an electron shuttle between Complex III (cytochrome c reductase) and IV (cytochrome c oxidase), but c-type cytochrome centers are also found in the active sites of many enzymes; Cytochrome c binds a heme as prosthetic group by Cys85 and Cys88. His89 is involved in iron binding; Belongs to class I (mono-heme) of Cytochrome c; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 16 and 17; Probably localized in the cytoplasmic and/or outer membrane; Funct [...]

NosL is one of the accessory lipoproteins of the nos (nitrous oxide reductase) gene cluster. NosL is a monomeric protein that specifically and stoichiometrically binds Cu(I). The copper ion in NosL is ligated by a Cys residue, and one Met and one His are thought to serve as the other ligands. It is possible that NosL is a copper chaperone involved in metallocenter assembly. Signal peptide cleaved between the residues 17 and 18. Localized in the outer membrane; High confidence in function and specificity.

Cytochromes c typically function in electron transfer. They are required during oxidative phosphorylation as an electron shuttle between Complex III (cytochrome c reductase) and IV (cytochrome c oxidase), but c-type cytochrome centers are also found in the active sites of many enzymes; Cytochrome c binds a heme as prosthetic group by Cys85 and Cys88. His89 is involved in iron binding; Belongs to class I (mono-heme) of Cytochrome c; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 16 and 17; Probably localized in the cytoplasmic and/or outer membrane; Funct [...]

Copper ABC importer, permease component; ABC (ATP-binding cassette) transporter, membrane domain. Proteins responsible for import of multi-copper across biological membranes. Contains six transmembrane segmemts; The proteins form homo- or hetero-oligomeric channels, allowing ATP-mediated transport; Localized in the cytoplasmic membrane; High confidence in function and specificity.

Cytochromes c typically function in electron transfer. They are required during oxidative phosphorylation as an electron shuttle between Complex III (cytochrome c reductase) and IV (cytochrome c oxidase), but c-type cytochrome centers are also found in the active sites of many enzymes; Cytochrome c binds a heme as prosthetic group by Cys85 and Cys88. His89 is involved in iron binding; Belongs to class I (mono-heme) of Cytochrome c; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 16 and 17; Probably localized in the cytoplasmic and/or outer membrane; Funct [...]

Nitrous-oxide reductase is a copper-containing enzyme that catalyses the two-electron reduction of the greenhouse gas N2O to N2. It is part of a bacterial respiratory system which is activated under anaerobic conditions in the presence of nitrate or nitrous oxide. Homodimer that Binds 6 copper ions per subunit. Signal peptide of lipoprotein cleaved between the residues 20 and 21. Localized in the cytoplasmic membrane; High confidence in function and specificity.

Conserved hypothetical membrane protein; Contains four transmembranes segments; Localized in the cytoplasmic membrane; Conserved hypothetical protein.

Cytochromes c typically function in electron transfer. They are required during oxidative phosphorylation as an electron shuttle between Complex III (cytochrome c reductase) and IV (cytochrome c oxidase), but c-type cytochrome centers are also found in the active sites of many enzymes; Cytochrome c binds a heme as prosthetic group by Cys85 and Cys88. His89 is involved in iron binding; Belongs to class I (mono-heme) of Cytochrome c; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 16 and 17; Probably localized in the cytoplasmic and/or outer membrane; Funct [...]

Conserved hypothetical membrane protein; Contains four transmembranes segments; Localized in the cytoplasmic membrane; Conserved hypothetical protein.

Conserved hypothetical membrane protein; Contains twelve transmembrane segments; Localized in the cytoplasmic membrane; Conserved hypothetical protein.

Conserved hypothetical membrane protein; Contains four transmembranes segments; Localized in the cytoplasmic membrane; Conserved hypothetical protein.

Copper-binding periplasmic protein; Protein which is thought to insert copper into the exported nitrous oxide reductase apoenzyme (NosZ). Belongs to the nitrous oxide reductase operon. Signal peptide cleaved between the residues 22 and 23. Localized in the periplasmic space; High confidence in function and specificity.

Conserved hypothetical membrane protein; Contains four transmembranes segments; Localized in the cytoplasmic membrane; Conserved hypothetical protein.

Copper ABC transporter, ATPase component; This protein, involved in copper processing/transport, is the nucleotide-binding domain of the ABC transporters (ABC ATPase); Responsible for coupling the energy of ATP hydrolysis to conformational changes in the permease component (ABC membrane). Belongs to the nitrous oxide reductase operon. It is a peripheral membrane protein localized near of the cytoplasmic membrane by association with the permease component; High confidence in function and specificity.

Conserved hypothetical membrane protein; Contains four transmembranes segments; Localized in the cytoplasmic membrane; Conserved hypothetical protein.

NosL is one of the accessory lipoproteins of the nos (nitrous oxide reductase) gene cluster. NosL is a monomeric protein that specifically and stoichiometrically binds Cu(I). The copper ion in NosL is ligated by a Cys residue, and one Met and one His are thought to serve as the other ligands. It is possible that NosL is a copper chaperone involved in metallocenter assembly. Signal peptide cleaved between the residues 17 and 18. Localized in the outer membrane; High confidence in function and specificity.

Conserved hypothetical membrane protein; Contains four transmembranes segments; Localized in the cytoplasmic membrane; Conserved hypothetical protein.

Copper ABC importer, permease component; ABC (ATP-binding cassette) transporter, membrane domain. Proteins responsible for import of multi-copper across biological membranes. Contains six transmembrane segmemts; The proteins form homo- or hetero-oligomeric channels, allowing ATP-mediated transport; Localized in the cytoplasmic membrane; High confidence in function and specificity.

Conserved hypothetical membrane protein; Contains four transmembranes segments; Localized in the cytoplasmic membrane; Conserved hypothetical protein.

Nitrous-oxide reductase is a copper-containing enzyme that catalyses the two-electron reduction of the greenhouse gas N2O to N2. It is part of a bacterial respiratory system which is activated under anaerobic conditions in the presence of nitrate or nitrous oxide. Homodimer that Binds 6 copper ions per subunit. Signal peptide of lipoprotein cleaved between the residues 20 and 21. Localized in the cytoplasmic membrane; High confidence in function and specificity.

Conserved hypothetical membrane protein; Contains twelve transmembrane segments; Localized in the cytoplasmic membrane; Conserved hypothetical protein.

Cytochromes c typically function in electron transfer. They are required during oxidative phosphorylation as an electron shuttle between Complex III (cytochrome c reductase) and IV (cytochrome c oxidase), but c-type cytochrome centers are also found in the active sites of many enzymes; Cytochrome c binds a heme as prosthetic group by Cys85 and Cys88. His89 is involved in iron binding; Belongs to class I (mono-heme) of Cytochrome c; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 16 and 17; Probably localized in the cytoplasmic and/or outer membrane; Funct [...]

Conserved hypothetical membrane protein; Contains twelve transmembrane segments; Localized in the cytoplasmic membrane; Conserved hypothetical protein.

Conserved hypothetical membrane protein; Contains four transmembranes segments; Localized in the cytoplasmic membrane; Conserved hypothetical protein.

Conserved hypothetical membrane protein; Contains twelve transmembrane segments; Localized in the cytoplasmic membrane; Conserved hypothetical protein.

Rieske [2Fe-2S] iron-sulfur protein; Protein that contains an unknown function N-terminal domain and a C-terminal Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines that one Fe ion while the other Fe ion is coordinated by two conserved histidines; Prokaryotic lipoprotein signal peptide cleaved between the residues 25 and 26; Localized in the outer membrane; Function unclear.