P26459 · APPC_ECOLI

  • Protein
    Cytochrome bd-II ubiquinol oxidase subunit 1
  • Gene
    appC
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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.

Caution

Was originally thought not to translocate protons.

Catalytic activity

Cofactor

heme (UniProtKB | Rhea| CHEBI:30413 )

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.

TypeIDPosition(s)Description
Binding site19Fe (UniProtKB | ChEBI) of heme 1 (UniProtKB | ChEBI); axial binding residue
Binding site186Fe (UniProtKB | ChEBI) of heme 2 (UniProtKB | ChEBI); axial binding residue
Binding site393Fe (UniProtKB | ChEBI) of heme 2 (UniProtKB | ChEBI); axial binding residue

GO annotations

AspectTerm
Cellular Componentcytochrome complex
Cellular Componentmembrane
Cellular Componentplasma membrane
Molecular Functioncytochrome bo3 ubiquinol oxidase activity
Molecular Functionelectron transfer activity
Molecular Functionheme binding
Molecular Functionmetal ion binding
Molecular Functionoxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor
Biological Processaerobic electron transport chain

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cytochrome bd-II ubiquinol oxidase subunit 1
  • EC number
  • Alternative names
    • Cytochrome bd-II oxidase subunit I

Gene names

    • Name
      appC
    • Synonyms
      cbdA, cyxA
    • Ordered locus names
      b0978, JW0960

Organism names

  • Taxonomic identifier
  • Strains
    • K12
    • K12 / W3110 / ATCC 27325 / DSM 5911
    • K12 / MG1655 / ATCC 47076
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    P26459

Proteomes

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-22Cytoplasmic
Transmembrane23-42Helical
Topological domain43-94Periplasmic
Transmembrane95-114Helical
Topological domain115-129Cytoplasmic
Transmembrane130-149Helical
Topological domain150-187Periplasmic
Transmembrane188-207Helical
Topological domain208-219Cytoplasmic
Transmembrane220-239Helical
Topological domain240-392Periplasmic
Transmembrane393-412Helical
Topological domain413-470Cytoplasmic
Transmembrane471-490Helical
Topological domain491-514Periplasmic

Keywords

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.

TypeIDPosition(s)Description
ChainPRO_00001839221-514Cytochrome bd-II ubiquinol oxidase subunit 1

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

View interactors in UniProtKB
View CPX-269 in Complex Portal

Protein-protein interaction databases

Family & Domains

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    514
  • Mass (Da)
    57,920
  • Last updated
    1992-08-01 v1
  • Checksum
    2D2FBD43429D960D
MWDVIDLSRWQFALTALYHFLFVPLTLGLIFLLAIMETIYVVTGKTIYRDMTRFWGKLFGINFALGVATGLTMEFQFGTNWSFYSNYVGDIFGAPLAMEALMAFFLESTFVGLFFFGWQRLNKYQHLLVTWLVAFGSNLSALWILNANGWMQYPTGAHFDIDTLRMEMTSFSELVFNPVSQVKFVHTVMAGYVTGAMFIMAISAWYLLRGRERNVALRSFAIGSVFGTLAIIGTLQLGDSSAYEVAQVQPVKLAAMEGEWQTEPAPAPFHVVAWPEQDQERNAFALKIPALLGILATHSLDKPVPGLKNLMAETYPRLQRGRMAWLLMQEISQGNREPHVLQAFRGLEGDLGYGMLLSRYAPDMNHVTAAQYQAAMRGAIPQVAPVFWSFRIMVGCGSLLLLVMLIALVQTLRGKIDQHRWVLKMALWSLPLPWIAIEAGWFMTEFGRQPWAIQDILPTYSAHSALTTGQLAFSLIMIVGLYTLFLIAEVYLMQKYARLGPSAMQSEQPTQQQG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp