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Protein

Cytochrome bd-II ubiquinol oxidase subunit 1

Gene

appC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

Catalytic activityi

2 ubiquinol + O2 + n H+(Side 1) = 2 ubiquinone + 2 H2O + n H+(Side 2).

Cofactori

hemeCuratedNote: May bind up to 3 heme groups per complex.Curated

Enzyme regulationi

Inhibited by cyanide; is more sensitive to cyanide than cytochrome bd-I oxidase.1 Publication

Pathwayi: oxidative phosphorylation

This protein is involved in the pathway oxidative phosphorylation, which is part of Energy metabolism.
View all proteins of this organism that are known to be involved in the pathway oxidative phosphorylation and in Energy metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi19 – 191Iron (heme 1 axial ligand)Sequence analysis
Metal bindingi186 – 1861Iron (heme 2 axial ligand)Sequence analysis
Metal bindingi393 – 3931Iron (heme 2 axial ligand)Sequence analysis

GO - Molecular functioni

  • electron carrier activity Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW
  • oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor Source: EcoCyc

GO - Biological processi

  • aerobic electron transport chain Source: EcoCyc
  • oxidative phosphorylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:APPC-MONOMER.
ECOL316407:JW0960-MONOMER.
MetaCyc:APPC-MONOMER.
UniPathwayiUPA00705.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome bd-II ubiquinol oxidase subunit 1 (EC:1.10.3.10)
Alternative name(s):
Cytochrome bd-II oxidase subunit I
Gene namesi
Name:appC
Synonyms:cbdA, cyxA
Ordered Locus Names:b0978, JW0960
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11380. appC.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2222CytoplasmicSequence analysisAdd
BLAST
Transmembranei23 – 4220HelicalSequence analysisAdd
BLAST
Topological domaini43 – 9452PeriplasmicSequence analysisAdd
BLAST
Transmembranei95 – 11420HelicalSequence analysisAdd
BLAST
Topological domaini115 – 12915CytoplasmicSequence analysisAdd
BLAST
Transmembranei130 – 14920HelicalSequence analysisAdd
BLAST
Topological domaini150 – 18738PeriplasmicSequence analysisAdd
BLAST
Transmembranei188 – 20720HelicalSequence analysisAdd
BLAST
Topological domaini208 – 21912CytoplasmicSequence analysisAdd
BLAST
Transmembranei220 – 23920HelicalSequence analysisAdd
BLAST
Topological domaini240 – 392153PeriplasmicSequence analysisAdd
BLAST
Transmembranei393 – 41220HelicalSequence analysisAdd
BLAST
Topological domaini413 – 47058CytoplasmicSequence analysisAdd
BLAST
Transmembranei471 – 49020HelicalSequence analysisAdd
BLAST
Topological domaini491 – 51424PeriplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytochrome complex Source: EcoCyc
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: UniProtKB
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

3-fold decreased ubiquinone levels but no change in redox levels of the ubiquinone pool (in aerobically grown minimal medium with glucose).3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 514514Cytochrome bd-II ubiquinol oxidase subunit 1PRO_0000183922Add
BLAST

Post-translational modificationi

The N-terminus is blocked.

Proteomic databases

PaxDbiP26459.
PRIDEiP26459.

Expressioni

Inductioni

Induced when bacterial cultures reach stationary phase; synthesis is triggered by phosphate starvation or a shift from aerobic to anaerobic conditions.1 Publication

Interactioni

Subunit structurei

Heterodimer of subunits I and II.1 Publication

Protein-protein interaction databases

BioGridi4260039. 178 interactions.
DIPiDIP-9119N.
IntActiP26459. 2 interactions.
STRINGi511145.b0978.

Structurei

3D structure databases

ProteinModelPortaliP26459.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105C4M. Bacteria.
COG1271. LUCA.
HOGENOMiHOG000084938.
InParanoidiP26459.
KOiK00425.
OMAiWGRLPKL.
OrthoDBiEOG600DNV.
PhylomeDBiP26459.

Family and domain databases

InterProiIPR002585. Cyt-d_ubiquinol_oxidase_su_1.
[Graphical view]
PfamiPF01654. Cyt_bd_oxida_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P26459-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWDVIDLSRW QFALTALYHF LFVPLTLGLI FLLAIMETIY VVTGKTIYRD
60 70 80 90 100
MTRFWGKLFG INFALGVATG LTMEFQFGTN WSFYSNYVGD IFGAPLAMEA
110 120 130 140 150
LMAFFLESTF VGLFFFGWQR LNKYQHLLVT WLVAFGSNLS ALWILNANGW
160 170 180 190 200
MQYPTGAHFD IDTLRMEMTS FSELVFNPVS QVKFVHTVMA GYVTGAMFIM
210 220 230 240 250
AISAWYLLRG RERNVALRSF AIGSVFGTLA IIGTLQLGDS SAYEVAQVQP
260 270 280 290 300
VKLAAMEGEW QTEPAPAPFH VVAWPEQDQE RNAFALKIPA LLGILATHSL
310 320 330 340 350
DKPVPGLKNL MAETYPRLQR GRMAWLLMQE ISQGNREPHV LQAFRGLEGD
360 370 380 390 400
LGYGMLLSRY APDMNHVTAA QYQAAMRGAI PQVAPVFWSF RIMVGCGSLL
410 420 430 440 450
LLVMLIALVQ TLRGKIDQHR WVLKMALWSL PLPWIAIEAG WFMTEFGRQP
460 470 480 490 500
WAIQDILPTY SAHSALTTGQ LAFSLIMIVG LYTLFLIAEV YLMQKYARLG
510
PSAMQSEQPT QQQG
Length:514
Mass (Da):57,920
Last modified:August 1, 1992 - v1
Checksum:i2D2FBD43429D960D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S63811 Genomic DNA. Translation: AAB20284.1.
U00096 Genomic DNA. Translation: AAC74063.1.
AP009048 Genomic DNA. Translation: BAA35743.1.
PIRiS17958.
RefSeqiNP_415497.1. NC_000913.3.
WP_000263582.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74063; AAC74063; b0978.
BAA35743; BAA35743; BAA35743.
GeneIDi945585.
KEGGiecj:JW0960.
eco:b0978.
PATRICi32117177. VBIEscCol129921_1012.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S63811 Genomic DNA. Translation: AAB20284.1.
U00096 Genomic DNA. Translation: AAC74063.1.
AP009048 Genomic DNA. Translation: BAA35743.1.
PIRiS17958.
RefSeqiNP_415497.1. NC_000913.3.
WP_000263582.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP26459.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260039. 178 interactions.
DIPiDIP-9119N.
IntActiP26459. 2 interactions.
STRINGi511145.b0978.

Proteomic databases

PaxDbiP26459.
PRIDEiP26459.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74063; AAC74063; b0978.
BAA35743; BAA35743; BAA35743.
GeneIDi945585.
KEGGiecj:JW0960.
eco:b0978.
PATRICi32117177. VBIEscCol129921_1012.

Organism-specific databases

EchoBASEiEB1354.
EcoGeneiEG11380. appC.

Phylogenomic databases

eggNOGiENOG4105C4M. Bacteria.
COG1271. LUCA.
HOGENOMiHOG000084938.
InParanoidiP26459.
KOiK00425.
OMAiWGRLPKL.
OrthoDBiEOG600DNV.
PhylomeDBiP26459.

Enzyme and pathway databases

UniPathwayiUPA00705.
BioCyciEcoCyc:APPC-MONOMER.
ECOL316407:JW0960-MONOMER.
MetaCyc:APPC-MONOMER.

Miscellaneous databases

PROiP26459.

Family and domain databases

InterProiIPR002585. Cyt-d_ubiquinol_oxidase_su_1.
[Graphical view]
PfamiPF01654. Cyt_bd_oxida_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A new oxygen-regulated operon in Escherichia coli comprises the genes for a putative third cytochrome oxidase and for pH 2.5 acid phosphatase (appA)."
    Dassa J., Fsihi H., Marck C., Dion M., Kieffer-Bontemps M., Boquet P.L.
    Mol. Gen. Genet. 229:341-352(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Purification of a cytochrome bd terminal oxidase encoded by the Escherichia coli app locus from a delta cyo delta cyd strain complemented by genes from Bacillus firmus OF4."
    Sturr M.G., Krulwich T.A., Hicks D.B.
    J. Bacteriol. 178:1742-1749(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN OXIDASE, ENZYME REGULATION, SUBUNIT, PROTEIN SEQUENCE OF 496-510.
  6. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: K12 / MG1655 / ATCC 47076.
  7. "Respiration of Escherichia coli can be fully uncoupled via the nonelectrogenic terminal cytochrome bd-II oxidase."
    Bekker M., de Vries S., Ter Beek A., Hellingwerf K.J., de Mattos M.J.
    J. Bacteriol. 191:5510-5517(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN OXIDASE, DISRUPTION PHENOTYPE.
    Strain: K12.
  8. "Aerobic respiratory chain of Escherichia coli is not allowed to work in fully uncoupled mode."
    Borisov V.B., Murali R., Verkhovskaya M.L., Bloch D.A., Han H., Gennis R.B., Verkhovsky M.I.
    Proc. Natl. Acad. Sci. U.S.A. 108:17320-17324(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN OXIDASE, FUNCTION IN PROTON TRANSLOCATION, DISRUPTION PHENOTYPE.
    Strain: K12.
  9. "Uncoupling of substrate-level phosphorylation in Escherichia coli during glucose-limited growth."
    Sharma P., Hellingwerf K.J., de Mattos M.J., Bekker M.
    Appl. Environ. Microbiol. 78:6908-6913(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN OXIDASE, FUNCTION IN PROTON TRANSLOCATION, DISRUPTION PHENOTYPE.
    Strain: K12.
  10. Cited for: REVIEW.

Entry informationi

Entry nameiAPPC_ECOLI
AccessioniPrimary (citable) accession number: P26459
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: January 20, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Was originally thought not to translocate protons.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.