P0ABJ1 (CYOA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquinol oxidase subunit 2
EC=1.10.3.-

Alternative name(s):
Cytochrome o subunit 2
Cytochrome o ubiquinol oxidase subunit 2
Short name=Ubiquinol oxidase chain B
Oxidase BO(3) subunit 2
Ubiquinol oxidase polypeptide II

Gene names

Name:	cyoA
Ordered Locus Names:	b0432, JW0422

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	315 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration.
Catalytic activity	Ubiquinol-8 + O2 = Ubiquinone-8 + H2O.
Subunit structure	Heterooctamer of two A chains, two B chains, two C chains and two D chains. Ref.10
Subcellular location	Cell inner membrane; Multi-pass membrane protein Ref.10.
Sequence similarities	Belongs to the cytochrome c oxidase subunit 2 family.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Oxidoreductase
PTM	Lipoprotein Palmitate
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	aerobic electron transport chain Inferred from mutant phenotype PubMed 2981797. Source: EcoCyc
Cellular_component	cytochrome o ubiquinol oxidase complex Inferred from direct assay PubMed 6308657. Source: EcoCyc integral to plasma membrane Inferred from direct assay PubMed 2162836. Source: EcoliWiki respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	copper ion binding Inferred from electronic annotation. Source: InterPro cytochrome bo3 ubiquinol oxidase activity Inferred from electronic annotation. Source: InterPro cytochrome o ubiquinol oxidase activity Inferred from electronic annotation. Source: InterPro cytochrome-c oxidase activity Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from direct assay PubMed 3301837. Source: EcoCyc hydrogen ion transmembrane transporter activity Inferred from direct assay Ref.13PubMed 2544445. Source: EcoCyc oxidoreduction-driven active transmembrane transporter activity Inferred from direct assay PubMed 6365921. Source: EcoCyc ubiquinone binding Inferred from direct assay PubMed 7961841. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

24

Potential

Chain

25 – 315

291

Ubiquinol oxidase subunit 2

PRO_0000006071

Regions

Topological domain

25 – 50

26

Periplasmic Probable

Transmembrane

51 – 68

18

Helical; Probable

Topological domain

69 – 92

24

Cytoplasmic Probable

Transmembrane

93 – 111

19

Helical; Probable

Topological domain

112 – 315

204

Periplasmic Probable

Amino acid modifications

Lipidation

25

1

N-palmitoyl cysteine Potential

Lipidation

25

1

S-diacylglycerol cysteine Potential

Secondary structure

1

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315

Helix Strand Turn

Details...

Helix

37 – 50

14

Turn

51 – 56

6

Helix

57 – 63

7

Turn

64 – 71

8

Turn

73 – 75

3

Helix

87 – 91

5

Helix

94 – 110

17

Beta strand

127 – 134

8

Beta strand

137 – 142

6

Turn

143 – 146

4

Beta strand

147 – 156

10

Beta strand

161 – 170

10

Beta strand

172 – 176

5

Helix

177 – 179

3

Beta strand

181 – 185

5

Beta strand

191 – 195

5

Beta strand

198 – 207

10

Turn

213 – 217

5

Beta strand

220 – 227

8

Helix

228 – 239

12

Helix

248 – 255

8

Beta strand

264 – 267

4

Helix

273 – 278

6

Turn

279 – 281

3

Sequences

	Sequence		Length	Mass (Da)
	P0ABJ1 [UniParc]. Last modified October 25, 2005. Version 1. Checksum: 62EC951183B65724	FASTA	315	34,911
	10 20 30 40 50 60 MRLRKYNKSL GWLSLFAGTV LLSGCNSALL DPKGQIGLEQ RSLILTAFGL MLIVVIPAIL 70 80 90 100 110 120 MAVGFAWKYR ASNKDAKYSP NWSHSNKVEA VVWTVPILII IFLAVLTWKT THALEPSKPL 130 140 150 160 170 180 AHDEKPITIE VVSMDWKWFF IYPEQGIATV NEIAFPANTP VYFKVTSNSV MNSFFIPRLG 190 200 210 220 230 240 SQIYAMAGMQ TRLHLIANEP GTYDGISASY SGPGFSGMKF KAIATPDRAA FDQWVAKAKQ 250 260 270 280 290 300 SPNTMSDMAA FEKLAAPSEY NQVEYFSNVK PDLFADVINK FMAHGKSMDM TQPEGEHSAH 310 EGMEGMDMSH AESAH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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]	"AmpG, a signal transducer in chromosomal beta-lactamase induction." Lindquist S., Weston-Hafer K., Schmidt H., Pul C., Korfmann G., Erickson J., Sanders C., Martin H.H., Normark S. Mol. Microbiol. 9:703-715(1993) [PubMed] [Europe PMC] [Abstract] 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]	"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.
[9]	"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.
[10]	"Protein complexes of the Escherichia coli cell envelope." Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O. J. Biol. Chem. 280:34409-34419(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, SUBCELLULAR LOCATION. Strain: BL21-DE3.
[11]	"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.
[12]	"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.
[13]	"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).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

A42226.

RefSeq

NP_414966.1. NC_000913.2.
YP_488724.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CYW	X-ray	2.50	A	111-315	[»]
1CYX	X-ray	2.30	A	111-315	[»]
1FFT	X-ray	3.50	B/G	1-315	[»]

ProteinModelPortal

P0ABJ1.

SMR

P0ABJ1. Positions 27-283.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47942N.

IntAct

P0ABJ1. 20 interactions.

STRING

511145.b0432.

Protein family/group databases

TCDB

3.D.4.5.1. proton-translocating cytochrome oxidase (COX) superfamily.

Proteomic databases

PaxDb

P0ABJ1.

PRIDE

P0ABJ1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73535; AAC73535; b0432.
BAE76212; BAE76212; BAE76212.

GeneID

12930518.
945080.

KEGG

ecj:Y75_p0420.
eco:b0432.

PATRIC

32116015. VBIEscCol129921_0449.

Organism-specific databases

EchoBASE

EB0175.

EcoGene

EG10178. cyoA.

Phylogenomic databases

eggNOG

COG1622.

HOGENOM

HOG000084157.

KO

K02297.

OMA

NKIFGML.

ProtClustDB

PRK10525.

Enzyme and pathway databases

BioCyc

EcoCyc:CYOA-MONOMER.
ECOL316407:JW0422-MONOMER.
MetaCyc:CYOA-MONOMER.

Gene expression databases

Genevestigator

P0ABJ1.

Family and domain databases

Gene3D

1.10.287.90. 1 hit.
2.60.40.420. 1 hit.

InterPro

IPR012141. Bo-type_Ubol_Oxase_su_II.
IPR010514. 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]

Pfam

PF00116. COX2. 1 hit.
PF06481. COX_ARM. 1 hit.
[Graphical view]

PIRSF

PIRSF000292. Ubi_od_II. 1 hit.

SUPFAM

SSF49503. Cupredoxin. 1 hit.
SSF81464. Cyt_c_oxidase_II-like_TM. 1 hit.

TIGRFAMs

TIGR01433. CyoA. 1 hit.

PROSITE

PS50857. COX2_CUA. 1 hit.
PS50999. COX2_TM. 1 hit.
PS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0ABJ1.

Entry information

Entry name

CYOA_ECOLI

Accession

Primary (citable) accession number: P0ABJ1
Secondary accession number(s): P18400, Q2MBZ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	October 25, 2005
Last modified:	May 1, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program