Q03736 (COX2_RHOSH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytochrome c oxidase subunit 2
EC=1.9.3.1

Alternative name(s):
Cytochrome aa3 subunit 2
Cytochrome c oxidase polypeptide II
Oxidase aa(3) subunit 2

Gene names

Name:	ctaC
Synonyms:	coxII, ctaB

Organism

Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides)

Taxonomic identifier

1063 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

Protein attributes

Sequence length	303 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	Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
Catalytic activity	4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O.
Cofactor	Copper A.
Subcellular location	Cell membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the cytochrome c oxidase subunit 2 family.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Cell membrane Membrane
Domain	Signal Transmembrane Transmembrane helix
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	copper ion binding Inferred from electronic annotation. Source: InterPro cytochrome-c oxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Potential

Chain

26 – 303

278

Cytochrome c oxidase subunit 2

PRO_0000006061

Regions

Transmembrane

60 – 80

21

Helical; Potential

Transmembrane

104 – 124

21

Helical; Potential

Sites

Metal binding

217

1

Copper A Probable

Metal binding

252

1

Copper A Probable

Metal binding

256

1

Copper A Probable

Metal binding

260

1

Copper A Probable

Secondary structure

1

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303

Helix Strand Turn

Details...

Beta strand

32 – 35

4

Helix

49 – 82

34

Turn

85 – 87

3

Helix

98 – 127

30

Beta strand

133 – 141

9

Beta strand

144 – 148

5

Turn

150 – 152

3

Beta strand

155 – 158

4

Helix

164 – 166

3

Helix

174 – 182

9

Helix

187 – 189

3

Turn

190 – 192

3

Beta strand

194 – 196

3

Beta strand

198 – 201

4

Beta strand

204 – 215

12

Beta strand

217 – 221

5

Helix

222 – 224

3

Beta strand

226 – 230

5

Beta strand

236 – 241

6

Beta strand

246 – 250

5

Helix

260 – 262

3

Beta strand

265 – 270

6

Helix

272 – 281

10

Helix

282 – 284

3

Sequences

	Sequence		Length	Mass (Da)
	Q03736 [UniParc]. Last modified May 27, 2002. Version 2. Checksum: 2F363ADA39EFEBF8	FASTA	303	32,931
	10 20 30 40 50 60 MRHSTTLTGC ATGAAGLLAA TAAAAQQQSL EIIGRPQPGG TGFQPSASPV ATQIHWLDGF 70 80 90 100 110 120 ILVIIAAITI FVTLLILYAV WRFHEKRNKV PARFTHNSPL EIAWTIVPIV ILVAIGAFSL 130 140 150 160 170 180 PVLFNQQEIP EADVTVKVTG YQWYWGYEYP DEEISFESYM IGSPATGGDN RMSPEVEQQL 190 200 210 220 230 240 IEAGYSRDEF LLATDTAMVV PVNKTVVVQV TGADVIHSWT VPAFGVKQDA VPGRLAQLWF 250 260 270 280 290 300 RAEREGIFFG QCSELCGISH AYMPITVKVV SEEAYAAWLE QARGGTYELS SVLPATPAGV SVE

References

[1]	"The gene encoding cytochrome c oxidase subunit II from Rhodobacter sphaeroides; comparison of the deduced amino acid sequence with sequences of corresponding peptides from other species." Cao J., Shapleigh J., Gennis R., Revzin A., Ferguson-Miller S. Gene 101:133-137(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	Hiser C., Ferguson-Miller S. Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M57680 Genomic DNA. Translation: AAA26100.3.

PIR

JQ1013.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M56	X-ray	2.30	B/H	26-289	[»]
1M57	X-ray	3.00	B/H	26-289	[»]
2GSM	X-ray	2.00	B/D	26-281	[»]
3DTU	X-ray	2.15	B/D	26-281	[»]
3FYE	X-ray	2.15	B/D	26-281	[»]
3FYI	X-ray	2.20	B/D	26-281	[»]

ProteinModelPortal

Q03736.

SMR

Q03736. Positions 30-289.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-38012N.

IntAct

Q03736. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

1.10.287.90. 1 hit.
2.60.40.420. 2 hits.

InterPro

IPR001505. Copper_CuA.
IPR008972. Cupredoxin.
IPR014222. Cyt_c_oxidase_su2.
IPR002429. Cyt_c_oxidase_su2_C.
IPR011759. Cyt_c_oxidase_su2_TM_dom.
[Graphical view]

Pfam

PF00116. COX2. 1 hit.
PF02790. COX2_TM. 1 hit.
[Graphical view]

SUPFAM

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

TIGRFAMs

TIGR02866. CoxB. 1 hit.

PROSITE

PS00078. COX2. 1 hit.
PS50857. COX2_CUA. 1 hit.
PS50999. COX2_TM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q03736.

Entry information

Entry name

COX2_RHOSH

Accession

Primary (citable) accession number: Q03736

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	May 27, 2002
Last modified:	May 1, 2013
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program