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Protein

Cytochrome bo(3) ubiquinol oxidase subunit 2

Gene

cyoA

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

Functioni

Cytochrome bo3 ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron.3 Publications

Enzyme regulationi

Competitively inhibited by piericidin A, non-competitively inhibited by 2-n-heptyl-4-hydroxyquinoline N-oxide, NaN3 and KCN; 50% inhibition occurs at 2 µM, 2 µM, 15 mM and 10 µM, respectively. Inhibited by Zn2+ and Cd2+.1 Publication

GO - Molecular functioni

  • copper ion binding Source: InterPro
  • cytochrome bo3 ubiquinol oxidase activity Source: EcoCyc
  • cytochrome-c oxidase activity Source: InterPro
  • cytochrome o ubiquinol oxidase activity Source: InterPro
  • electron carrier activity Source: EcoCyc
  • hydrogen ion transmembrane transporter activity Source: EcoCyc
  • oxidoreduction-driven active transmembrane transporter activity Source: EcoCyc
  • ubiquinone binding Source: EcoCyc

GO - Biological processi

  • aerobic electron transport chain Source: EcoCyc
  • aerobic respiration Source: EcoCyc
  • electron transport coupled proton transport Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Enzyme and pathway databases

BioCyciEcoCyc:CYOA-MONOMER.
ECOL316407:JW0422-MONOMER.
MetaCyc:CYOA-MONOMER.
BRENDAi1.10.3.10. 2026.

Protein family/group databases

TCDBi3.D.4.5.1. the proton-translocating cytochrome oxidase (cox) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome bo(3) ubiquinol oxidase subunit 2
Alternative name(s):
Cytochrome b562-o complex subunit II
Cytochrome o ubiquinol oxidase subunit 2
Short name:
Cytochrome o subunit 2
Oxidase bo(3) subunit 2
Ubiquinol oxidase chain B
Ubiquinol oxidase polypeptide II
Ubiquinol oxidase subunit 2
Gene namesi
Name:cyoA
Ordered Locus Names:b0432, JW0422
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10178. cyoA.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 5026PeriplasmicCuratedAdd
BLAST
Transmembranei51 – 6818HelicalCuratedAdd
BLAST
Topological domaini69 – 9224CytoplasmicCuratedAdd
BLAST
Transmembranei93 – 11119HelicalCuratedAdd
BLAST
Topological domaini112 – 315204PeriplasmicCuratedAdd
BLAST

GO - Cellular componenti

  • cytochrome o ubiquinol oxidase complex Source: EcoCyc
  • integral component of external side of plasma membrane Source: EcoCyc
  • integral component of plasma membrane Source: EcoliWiki
  • plasma membrane Source: EcoCyc
  • respiratory chain Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Increased reduction of the ubiquinone pool (in aerobically grown minimal medium with glucose).2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424PROSITE-ProRule annotationAdd
BLAST
Chaini25 – 315291Cytochrome bo(3) ubiquinol oxidase subunit 2PRO_0000006071Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi25 – 251N-palmitoyl cysteinePROSITE-ProRule annotation
Lipidationi25 – 251S-diacylglycerol cysteinePROSITE-ProRule annotation

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

EPDiP0ABJ1.
PaxDbiP0ABJ1.
PRIDEiP0ABJ1.

Interactioni

Subunit structurei

Heterooctamer of two A chains, two B chains, two C chains and two D chains.3 Publications

Protein-protein interaction databases

BioGridi4259512. 241 interactions.
DIPiDIP-47942N.
IntActiP0ABJ1. 23 interactions.
STRINGi511145.b0432.

Structurei

Secondary structure

1
315
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi37 – 5014Combined sources
Turni51 – 566Combined sources
Helixi57 – 637Combined sources
Turni64 – 718Combined sources
Turni73 – 753Combined sources
Helixi87 – 915Combined sources
Helixi94 – 11017Combined sources
Beta strandi127 – 1348Combined sources
Beta strandi137 – 1426Combined sources
Turni143 – 1464Combined sources
Beta strandi147 – 15610Combined sources
Beta strandi161 – 17010Combined sources
Beta strandi172 – 1765Combined sources
Helixi177 – 1793Combined sources
Beta strandi181 – 1855Combined sources
Beta strandi191 – 1955Combined sources
Beta strandi198 – 20710Combined sources
Turni213 – 2175Combined sources
Beta strandi220 – 2278Combined sources
Helixi228 – 23912Combined sources
Helixi248 – 2558Combined sources
Beta strandi264 – 2674Combined sources
Helixi273 – 2786Combined sources
Turni279 – 2813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CYWX-ray2.50A111-315[»]
1CYXX-ray2.30A111-315[»]
1FFTX-ray3.50B/G1-315[»]
DisProtiDP00089.
ProteinModelPortaliP0ABJ1.
SMRiP0ABJ1. Positions 27-283.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ABJ1.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105E2S. Bacteria.
COG1622. LUCA.
HOGENOMiHOG000084157.
InParanoidiP0ABJ1.
KOiK02297.
OMAiTAMNSFF.
OrthoDBiEOG6PS5TJ.
PhylomeDBiP0ABJ1.

Family and domain databases

Gene3Di1.10.287.90. 1 hit.
2.60.40.420. 1 hit.
InterProiIPR010514. COX_ARM.
IPR008972. Cupredoxin.
IPR002429. Cyt_c_oxidase_su2_C.
IPR011759. Cyt_c_oxidase_su2_TM_dom.
IPR006333. Cyt_o_ubiquinol_oxidase_su2.
[Graphical view]
PfamiPF00116. COX2. 1 hit.
PF06481. COX_ARM. 1 hit.
[Graphical view]
PIRSFiPIRSF000292. Ubi_od_II. 1 hit.
SUPFAMiSSF49503. SSF49503. 1 hit.
SSF81464. SSF81464. 1 hit.
TIGRFAMsiTIGR01433. CyoA. 1 hit.
PROSITEiPS50857. COX2_CUA. 1 hit.
PS50999. COX2_TM. 1 hit.
PS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0ABJ1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLRKYNKSL GWLSLFAGTV LLSGCNSALL DPKGQIGLEQ RSLILTAFGL
60 70 80 90 100
MLIVVIPAIL MAVGFAWKYR ASNKDAKYSP NWSHSNKVEA VVWTVPILII
110 120 130 140 150
IFLAVLTWKT THALEPSKPL AHDEKPITIE VVSMDWKWFF IYPEQGIATV
160 170 180 190 200
NEIAFPANTP VYFKVTSNSV MNSFFIPRLG SQIYAMAGMQ TRLHLIANEP
210 220 230 240 250
GTYDGISASY SGPGFSGMKF KAIATPDRAA FDQWVAKAKQ SPNTMSDMAA
260 270 280 290 300
FEKLAAPSEY NQVEYFSNVK PDLFADVINK FMAHGKSMDM TQPEGEHSAH
310
EGMEGMDMSH AESAH
Length:315
Mass (Da):34,911
Last modified:October 25, 2005 - v1
Checksum:i62EC951183B65724
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05492 Genomic DNA. Translation: AAA23631.1.
U82664 Genomic DNA. Translation: AAB40188.1.
U00096 Genomic DNA. Translation: AAC73535.1.
AP009048 Genomic DNA. Translation: BAE76212.1.
M55258 Genomic DNA. Translation: AAA23630.1.
S67816 Genomic DNA. Translation: AAB28885.1.
PIRiA42226.
RefSeqiNP_414966.1. NC_000913.3.
WP_001239436.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73535; AAC73535; b0432.
BAE76212; BAE76212; BAE76212.
GeneIDi945080.
KEGGiecj:JW0422.
eco:b0432.
PATRICi32116015. VBIEscCol129921_0449.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05492 Genomic DNA. Translation: AAA23631.1.
U82664 Genomic DNA. Translation: AAB40188.1.
U00096 Genomic DNA. Translation: AAC73535.1.
AP009048 Genomic DNA. Translation: BAE76212.1.
M55258 Genomic DNA. Translation: AAA23630.1.
S67816 Genomic DNA. Translation: AAB28885.1.
PIRiA42226.
RefSeqiNP_414966.1. NC_000913.3.
WP_001239436.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CYWX-ray2.50A111-315[»]
1CYXX-ray2.30A111-315[»]
1FFTX-ray3.50B/G1-315[»]
DisProtiDP00089.
ProteinModelPortaliP0ABJ1.
SMRiP0ABJ1. Positions 27-283.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259512. 241 interactions.
DIPiDIP-47942N.
IntActiP0ABJ1. 23 interactions.
STRINGi511145.b0432.

Protein family/group databases

TCDBi3.D.4.5.1. the proton-translocating cytochrome oxidase (cox) superfamily.

Proteomic databases

EPDiP0ABJ1.
PaxDbiP0ABJ1.
PRIDEiP0ABJ1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73535; AAC73535; b0432.
BAE76212; BAE76212; BAE76212.
GeneIDi945080.
KEGGiecj:JW0422.
eco:b0432.
PATRICi32116015. VBIEscCol129921_0449.

Organism-specific databases

EchoBASEiEB0175.
EcoGeneiEG10178. cyoA.

Phylogenomic databases

eggNOGiENOG4105E2S. Bacteria.
COG1622. LUCA.
HOGENOMiHOG000084157.
InParanoidiP0ABJ1.
KOiK02297.
OMAiTAMNSFF.
OrthoDBiEOG6PS5TJ.
PhylomeDBiP0ABJ1.

Enzyme and pathway databases

BioCyciEcoCyc:CYOA-MONOMER.
ECOL316407:JW0422-MONOMER.
MetaCyc:CYOA-MONOMER.
BRENDAi1.10.3.10. 2026.

Miscellaneous databases

EvolutionaryTraceiP0ABJ1.
PROiP0ABJ1.

Family and domain databases

Gene3Di1.10.287.90. 1 hit.
2.60.40.420. 1 hit.
InterProiIPR010514. COX_ARM.
IPR008972. Cupredoxin.
IPR002429. Cyt_c_oxidase_su2_C.
IPR011759. Cyt_c_oxidase_su2_TM_dom.
IPR006333. Cyt_o_ubiquinol_oxidase_su2.
[Graphical view]
PfamiPF00116. COX2. 1 hit.
PF06481. COX_ARM. 1 hit.
[Graphical view]
PIRSFiPIRSF000292. Ubi_od_II. 1 hit.
SUPFAMiSSF49503. SSF49503. 1 hit.
SSF81464. SSF81464. 1 hit.
TIGRFAMsiTIGR01433. CyoA. 1 hit.
PROSITEiPS50857. COX2_CUA. 1 hit.
PS50999. COX2_TM. 1 hit.
PS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The sequence of the cyo operon indicates substantial structural similarities between the cytochrome o ubiquinol oxidase of Escherichia coli and the aa3-type family of cytochrome c oxidases."
    Chepuri V., Lemieux L., Au D.C.T., Gennis R.B.
    J. Biol. Chem. 265:11185-11192(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  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. "Transcriptional regulation of the cytochrome b562-o complex in Escherichia coli. Gene expression and molecular characterization of the promoter."
    Minagawa J., Nakamura H., Yamato I., Mogi T., Anraku Y.
    J. Biol. Chem. 265:11198-11203(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
  6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-66.
  7. "Modified, large-scale purification of the cytochrome o complex (bo-type oxidase) of Escherichia coli yields a two heme/one copper terminal oxidase with high specific activity."
    Minghetti K.C., Goswitz V.C., Gabriel N.E., Hill J.J., Barassi C.A., Georgiou C.D., Chan S.I., Gennis R.B.
    Biochemistry 31:6917-6924(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 153-171.
  8. "Reconstitution of active transport in proteoliposomes containing cytochrome o oxidase and lac carrier protein purified from Escherichia coli."
    Matsushita K., Patel L., Gennis R.B., Kaback H.R.
    Proc. Natl. Acad. Sci. U.S.A. 80:4889-4893(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN UBIQUINOL OXIDATION, FUNCTION IN PROTON ELECTROCHEMICAL GRADIENT GENERATION, SUBUNIT.
  9. "Terminal oxidases of Escherichia coli aerobic respiratory chain. I. Purification and properties of cytochrome b562-o complex from cells in the early exponential phase of aerobic growth."
    Kita K., Konishi K., Anraku Y.
    J. Biol. Chem. 259:3368-3374(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, SUBCELLULAR LOCATION.
    Strain: K12 / KL251/ORF4.
  10. "The use of gene fusions to determine the topology of all of the subunits of the cytochrome o terminal oxidase complex of Escherichia coli."
    Chepuri V., Gennis R.B.
    J. Biol. Chem. 265:12978-12986(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.
  11. "Recent studies of the cytochrome o terminal oxidase complex of Escherichia coli."
    Chepuri V., Lemieux L., Hill J., Alben J.O., Gennis R.B.
    Biochim. Biophys. Acta 1018:124-127(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.
  12. Cited for: SUBUNIT, SUBCELLULAR LOCATION.
    Strain: BL21-DE3.
  13. "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: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: K12 / MG1655 / ATCC 47076.
  14. "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, FUNCTION AS A PROTON PUMP, DISRUPTION PHENOTYPE.
    Strain: K12.
  15. "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.
  16. "Crystal structure of the membrane-exposed domain from a respiratory quinol oxidase complex with an engineered dinuclear copper center."
    Wilmanns M., Lappalainen P., Kelly M., Sauer-Eriksson E., Saraste M.
    Proc. Natl. Acad. Sci. U.S.A. 92:11955-11959(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 111-315.
  17. "The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site."
    Abramson J., Riistama S., Larsson G., Jasaitis A., Svensson-Ek M., Puustinen A., Iwata S., Wikstrom M.
    Nat. Struct. Biol. 7:910-917(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS), SUBUNIT.

Entry informationi

Entry nameiCYOA_ECOLI
AccessioniPrimary (citable) accession number: P0ABJ1
Secondary accession number(s): P18400, Q2MBZ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: March 16, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.