P0ABI8 (CYOB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquinol oxidase subunit 1
EC=1.10.3.-

Alternative name(s):
Cytochrome o subunit 1
Cytochrome o ubiquinol oxidase subunit 1
Oxidase BO(3) subunit 1
Ubiquinol oxidase chain A
Ubiquinol oxidase polypeptide I

Gene names

Name:	cyoB
Ordered Locus Names:	b0431, JW0421

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	663 AA.
Sequence status	Complete.
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. This ubiquinol oxidase shows proton pump activity across the membrane in addition to the electron transfer.
Catalytic activity	Ubiquinol-8 + O2 = Ubiquinone-8 + H2O.
Cofactor	Binds 1 copper ion. Binds 2 protoheme IX (heme b55 and b562) groups.
Subunit structure	Heterooctamer of two A chains, two B chains, two C chains and two D chains.
Subcellular location	Cell inner membrane; Multi-pass membrane protein.
Miscellaneous	Ubiquinol oxidase catalyzes the terminal step in the electron transport chain.
Sequence similarities	Belongs to the heme-copper respiratory oxidase family.

Ontologies

Keywords
Biological process	Electron transport Hydrogen ion transport Ion transport Respiratory chain Transport
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Copper Heme Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aerobic electron transport chain Inferred from mutant phenotype PubMed 2981797. Source: EcoCyc electron transport coupled proton transport Inferred from mutant phenotype PubMed 2544445. 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 direct assay Ref.9PubMed 6365921. Source: EcoCyc cytochrome bo3 ubiquinol oxidase activity Inferred from direct assay PubMed 1322173. Source: EcoCyc cytochrome-c oxidase activity Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from direct assay PubMed 3301837. Source: EcoCyc heme binding Inferred from direct assay Ref.9PubMed 6365921. Source: EcoCyc hydrogen ion transmembrane transporter activity Inferred from direct assay Ref.9. Source: EcoCyc iron ion binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor Inferred from electronic annotation. Source: InterPro oxidoreduction-driven active transmembrane transporter activity Inferred from direct assay PubMed 6365921. Source: EcoCyc ubiquinone binding Inferred from direct assay Ref.9. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 663

663

Ubiquinol oxidase subunit 1

PRO_0000183476

Regions

Topological domain

1 – 16

16

Periplasmic Ref.5 Ref.6 Ref.8

Transmembrane

17 – 35

19

Helical; Name=I

Topological domain

36 – 52

17

Cytoplasmic Ref.5 Ref.6 Ref.8

Transmembrane

53 – 80

28

Helical; Name=II

Topological domain

81 – 95

15

Periplasmic Ref.5 Ref.6 Ref.8

Transmembrane

96 – 132

37

Helical; Name=III

Topological domain

133 – 137

5

Cytoplasmic Ref.5 Ref.6 Ref.8

Transmembrane

138 – 161

24

Helical; Name=IV

Topological domain

162 – 184

23

Periplasmic Ref.5 Ref.6 Ref.8

Transmembrane

185 – 215

31

Helical; Name=V

Topological domain

216 – 224

9

Cytoplasmic Ref.5 Ref.6 Ref.8

Transmembrane

225 – 260

36

Helical; Name=VI

Topological domain

261 – 270

10

Periplasmic Ref.5 Ref.6 Ref.8

Transmembrane

271 – 307

37

Helical; Name=VII

Topological domain

308 – 311

4

Cytoplasmic Ref.5 Ref.6 Ref.8

Transmembrane

312 – 326

15

Helical; Name=VIII

Topological domain

327 – 340

14

Periplasmic Ref.5 Ref.6 Ref.8

Transmembrane

341 – 369

29

Helical; Name=IX

Topological domain

370 – 377

8

Cytoplasmic Ref.5 Ref.6 Ref.8

Transmembrane

378 – 409

32

Helical; Name=X

Topological domain

410 – 412

3

Periplasmic Ref.5 Ref.6 Ref.8

Transmembrane

413 – 445

33

Helical; Name=XI

Topological domain

446 – 448

3

Cytoplasmic Ref.5 Ref.6 Ref.8

Transmembrane

449 – 477

29

Helical; Name=XII

Topological domain

478 – 489

12

Periplasmic Ref.5 Ref.6 Ref.8

Transmembrane

490 – 521

32

Helical; Name=XIII

Topological domain

522 – 587

66

Cytoplasmic Ref.5 Ref.6 Ref.8

Transmembrane

588 – 606

19

Helical; Name=XIV

Topological domain

607 – 613

7

Periplasmic Ref.5 Ref.6 Ref.8

Transmembrane

614 – 632

19

Helical; Name=XV

Topological domain

633 – 663

31

Cytoplasmic Ref.5 Ref.6 Ref.8

Sites

Metal binding

106

1

Iron (heme B axial ligand) Probable

Metal binding

284

1

Copper B Probable

Metal binding

288

1

Copper B Probable

Metal binding

333

1

Copper B Probable

Metal binding

334

1

Copper B Probable

Metal binding

419

1

Iron (heme O axial ligand) Probable

Metal binding

421

1

Iron (heme B axial ligand) Probable

Amino acid modifications

Cross-link

284 ↔ 288

1'-histidyl-3'-tyrosine (His-Tyr) By similarity

Experimental info

Mutagenesis

55

1

K → Q: No effect. Ref.7

Mutagenesis

71

1

R → Q or L: Abolishes enzyme activity. Ref.9

Mutagenesis

75

1

D → N: Abolishes enzyme activity. Ref.9

Mutagenesis

80

1

R → Q: Abolishes enzyme activity. Ref.7

Mutagenesis

98

1

H → N: Abolishes enzyme activity. Ref.9

Mutagenesis

101

1

Q → N: Reduces enzyme activity by 75%. Ref.9

Mutagenesis

135

1

D → N: Abolishes enzyme activity. Ref.7

Mutagenesis

173

1

Y → F: No effect. Ref.7

Mutagenesis

188

1

D → N: No effect. Ref.7

Mutagenesis

256

1

D → N: No effect.

Mutagenesis

257

1

R → Q: Abolishes enzyme activity.

Mutagenesis

286

1

E → Q or D: Great decrease in activity. Ref.7

Mutagenesis

288

1

Y → F: Great decrease in activity. Ref.7

Mutagenesis

362

1

K → Q: Abolishes enzyme activity. Ref.7

Mutagenesis

407

1

D → N: Abolishes enzyme activity. Ref.7

Mutagenesis

481

1

R → Q: No effect.

Mutagenesis

482

1

R → Q: No effect.

Mutagenesis

540

1

E → Q: Abolishes enzyme activity. Ref.7

Secondary structure

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663

Helix Strand Turn

Details...

Helix

54 – 79

26

Turn

80 – 84

5

Beta strand

85 – 88

4

Helix

97 – 112

16

Helix

117 – 131

15

Helix

139 – 160

22

Turn

161 – 163

3

Turn

169 – 172

4

Turn

174 – 176

3

Helix

186 – 214

29

Helix

222 – 224

3

Helix

227 – 241

15

Helix

244 – 259

16

Turn

266 – 269

4

Helix

272 – 289

18

Helix

292 – 306

15

Helix

313 – 325

13

Helix

331 – 334

4

Turn

335 – 339

5

Helix

342 – 354

13

Helix

357 – 368

12

Turn

369 – 372

4

Helix

379 – 401

23

Helix

404 – 408

5

Turn

409 – 412

4

Helix

414 – 425

12

Turn

426 – 428

3

Helix

429 – 444

16

Helix

450 – 476

27

Helix

491 – 520

30

Turn

539 – 542

4

Sequences

	Sequence		Length	Mass (Da)
	P0ABI8 [UniParc]. Last modified October 25, 2005. Version 1. Checksum: 17357B8D44C7CF84	FASTA	663	74,368
	10 20 30 40 50 60 MFGKLSLDAV PFHEPIVMVT IAGIILGGLA LVGLITYFGK WTYLWKEWLT SVDHKRLGIM 70 80 90 100 110 120 YIIVAIVMLL RGFADAIMMR SQQALASAGE AGFLPPHHYD QIFTAHGVIM IFFVAMPFVI 130 140 150 160 170 180 GLMNLVVPLQ IGARDVAFPF LNNLSFWFTV VGVILVNVSL GVGEFAQTGW LAYPPLSGIE 190 200 210 220 230 240 YSPGVGVDYW IWSLQLSGIG TTLTGINFFV TILKMRAPGM TMFKMPVFTW ASLCANVLII 250 260 270 280 290 300 ASFPILTVTV ALLTLDRYLG THFFTNDMGG NMMMYINLIW AWGHPEVYIL ILPVFGVFSE 310 320 330 340 350 360 IAATFSRKRL FGYTSLVWAT VCITVLSFIV WLHHFFTMGA GANVNAFFGI TTMIIAIPTG 370 380 390 400 410 420 VKIFNWLFTM YQGRIVFHSA MLWTIGFIVT FSVGGMTGVL LAVPGADFVL HNSLFLIAHF 430 440 450 460 470 480 HNVIIGGVVF GCFAGMTYWW PKAFGFKLNE TWGKRAFWFW IIGFFVAFMP LYALGFMGMT 490 500 510 520 530 540 RRLSQQIDPQ FHTMLMIAAS GAVLIALGIL CLVIQMYVSI RDRDQNRDLT GDPWGGRTLE 550 560 570 580 590 600 WATSSPPPFY NFAVVPHVHE RDAFWEMKEK GEAYKKPDHY EEIHMPKNSG AGIVIAAFST 610 620 630 640 650 660 IFGFAMIWHI WWLAIVGFAG MIITWIVKSF DEDVDYYVPV AEIEKLENQH FDEITKAGLK NGN

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].
[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]	"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.
[6]	"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.
[7]	"Substitutions of charged amino acid residues conserved in subunit I perturb the redox metal centers of the Escherichia coli bo-type ubiquinol oxidase." Kawasaki M., Mogi T., Anraku Y. J. Biochem. 122:422-429(1997) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF LYS-55; ARG-80; ASP-135; TYR-173; ASP-188; 256-ASP-ARG-257; GLU-286; TYR-288; LYS-362; ASP-407; 481-ARG-ARG-482 AND GLU-540.
[8]	"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.
[9]	"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), MUTAGENESIS OF ARG-71; ASP-75; HIS-98 AND GLN-101.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J05492 Genomic DNA. Translation: AAA23632.1.
U82664 Genomic DNA. Translation: AAB40187.1.
U00096 Genomic DNA. Translation: AAC73534.1.
AP009048 Genomic DNA. Translation: BAE76211.1.

PIR

B42226.

RefSeq

NP_414965.1. NC_000913.2.
YP_488723.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FFT	X-ray	3.50	A/F	1-663	[»]

ProteinModelPortal

P0ABI8.

SMR

P0ABI8. Positions 41-628.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47943N.

IntAct

P0ABI8. 1 interaction.

STRING

511145.b0431.

Protein family/group databases

TCDB

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

Proteomic databases

PaxDb

P0ABI8.

PRIDE

P0ABI8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73534; AAC73534; b0431.
BAE76211; BAE76211; BAE76211.

GeneID

12930716.
945615.

KEGG

ecj:Y75_p0419.
eco:b0431.

PATRIC

32116013. VBIEscCol129921_0448.

Organism-specific databases

EchoBASE

EB0176.

EcoGene

EG10179. cyoB.

Phylogenomic databases

eggNOG

COG0843.

HOGENOM

HOG000085275.

KO

K02298.

OMA

WNIWLYI.

ProtClustDB

PRK15017.

Enzyme and pathway databases

BioCyc

EcoCyc:CYOB-MONOMER.
ECOL316407:JW0421-MONOMER.
MetaCyc:CYOB-MONOMER.

Gene expression databases

Genevestigator

P0ABI8.

Family and domain databases

Gene3D

1.20.210.10. 1 hit.

InterPro

IPR000883. Cyt_c_Oxase_su1.
IPR023615. Cyt_c_Oxase_su1_BS.
IPR023616. Cyt_c_Oxase_su1_dom.
IPR014207. Cyt_c_ubiqinol_oxidase_su1.
[Graphical view]

PANTHER

PTHR10422. PTHR10422. 1 hit.

Pfam

PF00115. COX1. 1 hit.
[Graphical view]

PRINTS

PR01165. CYCOXIDASEI.

SUPFAM

SSF81442. COX1. 1 hit.

TIGRFAMs

TIGR02843. CyoB. 1 hit.

PROSITE

PS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0ABI8.

Entry information

Entry name

CYOB_ECOLI

Accession

Primary (citable) accession number: P0ABI8
Secondary accession number(s): P18401, Q2MBZ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	October 25, 2005
Last modified:	May 1, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program