Cytochrome c oxidase subunit 2 precursor - Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)

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Q8NNK2 (COX2_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 91. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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
Ordered Locus Names:	Cgl2195, cg2409

Organism

Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]

Taxonomic identifier

196627 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium ›

Protein attributes

Sequence length	359 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) By similarity.
Catalytic activity	4 ferrocytochrome c + O₂ + 4 H⁺ = 4 ferricytochrome c + 2 H₂O.
Cofactor	Binds 2 copper A ions per subunit By similarity.
Subunit structure	Associates with subunits I, III and IV to form cytochrome c oxidase. The 4 subunit cytochrome c oxidase forms a supercomplex with the menaquinol-cytochrome c reductase complex (cytochrome bc1). Ref.1
Subcellular location	Cell membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the cytochrome c oxidase subunit 2 family.
Mass spectrometry	Molecular mass is 37314.7±83.2 Da from positions 29 - 359. Determined by MALDI. Ref.1

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
PTM	Lipoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
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 – 28

Ref.1

Chain

29 – 359

331

Cytochrome c oxidase subunit 2

PRO_0000006054

Regions

Transmembrane

64 – 84

Helical; Potential

Transmembrane

107 – 127

Helical; Potential

Sites

Metal binding

244

Copper A1 By similarity

Metal binding

285

Copper A1 By similarity

Metal binding

285

Copper A2 By similarity

Metal binding

287

Copper A2; via carbonyl oxygen By similarity

Metal binding

289

Copper A1 By similarity

Metal binding

289

Copper A2 By similarity

Metal binding

293

Copper A2 By similarity

Metal binding

296

Copper A1 By similarity

Site

Not N-palmitoylated

Amino acid modifications

Lipidation

S-diacylglycerol cysteine

Experimental info

Sequence conflict

W → C in BAB64407. Ref.1

Sequence conflict

310

E → V in BAB64407. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q8NNK2 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 5BB65F6AB2BE493A
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FASTA

359

39,632

        10         20         30         40         50         60 
MEQQNKRGLK RKALLGGVLG LGGLAMAGCE VAPPGGVLGD FLRMGWPDGI TPEAVAMGNF 

        70         80         90        100        110        120 
WSWVWVAAWI IGIIMWGLFL TAIFAWGAKR AEKRGEGEFP KQLQYNVPLE LVLTIVPIII 

       130        140        150        160        170        180 
VMVLFFFTVQ TQDKVTALDK NPEVTVDVTA YQWNWKFGYS EIDGSLAPGG QDYQGSDPER 

       190        200        210        220        230        240 
QAAAEASKKD PSGDNPIHGN SKSDVSYLEF NRIETLGTTD EIPVMVLPVN TPIEFNLASA 

       250        260        270        280        290        300 
DVAHSFWVPE FLFKRDAYAH PEANKSQRVF QIEEITEEGA FVGRCAEMCG TYHAMMNFEL 

       310        320        330        340        350 
RVVDRDSFAE YISFRDSNPD ATNAQALEHI GQAPYATSTS PFVSDRTATR DGENTQSNA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cytochrome c oxidase contains an extra charged amino acid cluster in a new type of respiratory chain in the amino acid-producing Gram-positive bacterium Corynebacterium glutamicum." Sakamoto J., Shibata T., Mine T., Miyahara R., Torigoe T., Noguchi S., Matsushita K., Sone N. Microbiology 147:2865-2871(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 29-50, SUBUNIT, HEME CHARACTERIZATION, MASS SPECTROMETRY. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]	"The Corynebacterium glutamicum genome: features and impacts on biotechnological processes." Ikeda M., Nakagawa S. Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[3]	"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. Tauch A. J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[4]	"Purification of a cytochrome bc1-aa3 supercomplex with quinol oxidase activity from Corynebacterium glutamicum. Identification of a fourth subunity of cytochrome aa3 oxidase and mutational analysis of diheme cytochrome c1." Niebisch A., Bott M. J. Biol. Chem. 278:4339-4346(2003) [PubMed] [Europe PMC] [Abstract] Cited for: DETECTION IN A SUPERCOMPLEX WITH MENAQUINOL-CYTOCHROME C REDUCTASE (CYTOCHROME BC1). Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB052749 Genomic DNA. Translation: BAB64407.1. BA000036 Genomic DNA. Translation: BAB99588.1. BX927154 Genomic DNA. Translation: CAF20536.1.
RefSeq	NP_601399.1. NC_003450.3. YP_226437.1. NC_006958.1.
3D structure databases
ProteinModelPortal	Q8NNK2.
ModBase	Search...
Protein-protein interaction databases
STRING	196627.cg2409.
Protein family/group databases
TCDB	3.D.4.4.2. proton-translocating cytochrome oxidase (COX) superfamily.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB99588; BAB99588; BAB99588. CAF20536; CAF20536; cg2409.
GeneID	1020147. 3345096.
KEGG	cgb:cg2409. cgl:NCgl2115.
PATRIC	21496390. VBICorGlu203724_2131.
Phylogenomic databases
eggNOG	COG1622.
HOGENOM	HOG000245527.
KO	K02275.
OMA	MRELWTW.
ProtClustDB	CLSK2518737.
Enzyme and pathway databases
BioCyc	CGLU196627:GJDM-2169-MONOMER.
Family and domain databases
Gene3D	1.10.287.90. 1 hit. 2.60.40.420. 2 hits.
InterPro	IPR001505. Copper_CuA. IPR008972. Cupredoxin. IPR002429. Cyt_c_oxidase_su2_C. IPR011759. Cyt_c_oxidase_su2_TM_dom. [Graphical view]
Pfam	PF00116. COX2. 1 hit. [Graphical view]
SUPFAM	SSF49503. Cupredoxin. 1 hit. SSF81464. Cyt_c_oxidase_II-like_TM. 1 hit.
PROSITE	PS00078. COX2. 1 hit. PS50857. COX2_CUA. 1 hit. PS50999. COX2_TM. 1 hit. PS51257. PROKAR_LIPOPROTEIN. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

COX2_CORGL

Accession

Primary (citable) accession number: Q8NNK2
Secondary accession number(s): Q6M3N8, Q93HZ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	October 1, 2002
Last modified:	May 1, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents