P26459 · APPC_ECOLI
- ProteinCytochrome bd-II ubiquinol oxidase subunit 1
- GeneappC
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids514 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
A terminal oxidase that catalyzes quinol-dependent, Na+-independent oxygen uptake. Prefers menadiol over other quinols although ubiquinol was not tested (PubMed:8626304).
Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H2O, transferring 1 proton/electron.
Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H2O, transferring 1 proton/electron.
Catalytic activity
- 2 a ubiquinol + O2 + n H+(in) = 2 a ubiquinone + 2 H2O + n H+(out)
2 a ubiquinol RHEA-COMP:9566 + CHEBI:15379 + n H+ (in)CHEBI:15378= 2 a ubiquinone RHEA-COMP:9565 + 2 CHEBI:15377 + n H+ (out)CHEBI:15378
Cofactor
Note: May bind up to 3 heme groups per complex.
Activity regulation
Inhibited by cyanide; is more sensitive to cyanide than cytochrome bd-I oxidase.
Pathway
Energy metabolism; oxidative phosphorylation.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 19 | Fe (UniProtKB | ChEBI) of heme 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 186 | Fe (UniProtKB | ChEBI) of heme 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 393 | Fe (UniProtKB | ChEBI) of heme 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: M |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytochrome complex | |
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Molecular Function | cytochrome bo3 ubiquinol oxidase activity | |
Molecular Function | electron transfer activity | |
Molecular Function | heme binding | |
Molecular Function | metal ion binding | |
Molecular Function | oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor | |
Biological Process | aerobic electron transport chain |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCytochrome bd-II ubiquinol oxidase subunit 1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP26459
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-22 | Cytoplasmic | ||||
Sequence: MWDVIDLSRWQFALTALYHFLF | ||||||
Transmembrane | 23-42 | Helical | ||||
Sequence: VPLTLGLIFLLAIMETIYVV | ||||||
Topological domain | 43-94 | Periplasmic | ||||
Sequence: TGKTIYRDMTRFWGKLFGINFALGVATGLTMEFQFGTNWSFYSNYVGDIFGA | ||||||
Transmembrane | 95-114 | Helical | ||||
Sequence: PLAMEALMAFFLESTFVGLF | ||||||
Topological domain | 115-129 | Cytoplasmic | ||||
Sequence: FFGWQRLNKYQHLLV | ||||||
Transmembrane | 130-149 | Helical | ||||
Sequence: TWLVAFGSNLSALWILNANG | ||||||
Topological domain | 150-187 | Periplasmic | ||||
Sequence: WMQYPTGAHFDIDTLRMEMTSFSELVFNPVSQVKFVHT | ||||||
Transmembrane | 188-207 | Helical | ||||
Sequence: VMAGYVTGAMFIMAISAWYL | ||||||
Topological domain | 208-219 | Cytoplasmic | ||||
Sequence: LRGRERNVALRS | ||||||
Transmembrane | 220-239 | Helical | ||||
Sequence: FAIGSVFGTLAIIGTLQLGD | ||||||
Topological domain | 240-392 | Periplasmic | ||||
Sequence: SSAYEVAQVQPVKLAAMEGEWQTEPAPAPFHVVAWPEQDQERNAFALKIPALLGILATHSLDKPVPGLKNLMAETYPRLQRGRMAWLLMQEISQGNREPHVLQAFRGLEGDLGYGMLLSRYAPDMNHVTAAQYQAAMRGAIPQVAPVFWSFRI | ||||||
Transmembrane | 393-412 | Helical | ||||
Sequence: MVGCGSLLLLVMLIALVQTL | ||||||
Topological domain | 413-470 | Cytoplasmic | ||||
Sequence: RGKIDQHRWVLKMALWSLPLPWIAIEAGWFMTEFGRQPWAIQDILPTYSAHSALTTGQ | ||||||
Transmembrane | 471-490 | Helical | ||||
Sequence: LAFSLIMIVGLYTLFLIAEV | ||||||
Topological domain | 491-514 | Periplasmic | ||||
Sequence: YLMQKYARLGPSAMQSEQPTQQQG |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
3-fold decreased ubiquinone levels but no change in redox levels of the ubiquinone pool (in aerobically grown minimal medium with glucose).
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000183922 | 1-514 | Cytochrome bd-II ubiquinol oxidase subunit 1 | |||
Sequence: MWDVIDLSRWQFALTALYHFLFVPLTLGLIFLLAIMETIYVVTGKTIYRDMTRFWGKLFGINFALGVATGLTMEFQFGTNWSFYSNYVGDIFGAPLAMEALMAFFLESTFVGLFFFGWQRLNKYQHLLVTWLVAFGSNLSALWILNANGWMQYPTGAHFDIDTLRMEMTSFSELVFNPVSQVKFVHTVMAGYVTGAMFIMAISAWYLLRGRERNVALRSFAIGSVFGTLAIIGTLQLGDSSAYEVAQVQPVKLAAMEGEWQTEPAPAPFHVVAWPEQDQERNAFALKIPALLGILATHSLDKPVPGLKNLMAETYPRLQRGRMAWLLMQEISQGNREPHVLQAFRGLEGDLGYGMLLSRYAPDMNHVTAAQYQAAMRGAIPQVAPVFWSFRIMVGCGSLLLLVMLIALVQTLRGKIDQHRWVLKMALWSLPLPWIAIEAGWFMTEFGRQPWAIQDILPTYSAHSALTTGQLAFSLIMIVGLYTLFLIAEVYLMQKYARLGPSAMQSEQPTQQQG |
Post-translational modification
The N-terminus is blocked.
Proteomic databases
Expression
Induction
Induced when bacterial cultures reach stationary phase; synthesis is triggered by phosphate starvation or a shift from aerobic to anaerobic conditions.
Interaction
Subunit
Heterodimer of subunits I and II.
Complex viewer
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length514
- Mass (Da)57,920
- Last updated1992-08-01 v1
- Checksum2D2FBD43429D960D
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
S63811 EMBL· GenBank· DDBJ | AAB20284.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC74063.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAA35743.1 EMBL· GenBank· DDBJ | Genomic DNA |