P63855 (COX2_MYCBO) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 67.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames 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 | ||||
| Gene names |
| ||||
| Organism | Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 233413 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › ![]() |
Protein attributes
| Sequence length | 363 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
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 | Copper A By similarity. Heme group By similarity. |
| Subcellular location | Cell membrane; Multi-pass membrane protein Potential. |
| 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 Heme Iron Metal-binding |
| Molecular function | Oxidoreductase |
| Technical term | Complete 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 membraneInferred from electronic annotation. Source: UniProtKB-SubCell respiratory chainInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | copper ion binding Inferred from electronic annotation. Source: InterPro cytochrome-c oxidase activityInferred 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 – 41 | 41 | Potential | ||||||
| Chain | 42 – 363 | 322 | Cytochrome c oxidase subunit 2 | PRO_0000006055 | |||||
Regions | |||||||||
| Transmembrane | 71 – 91 | 21 | Helical; Potential | ||||||
| Transmembrane | 118 – 138 | 21 | Helical; Potential | ||||||
Sites | |||||||||
| Metal binding | 254 | 1 | Copper A Potential | ||||||
| Metal binding | 295 | 1 | Copper A Potential | ||||||
| Metal binding | 299 | 1 | Copper A Potential | ||||||
| Metal binding | 303 | 1 | Copper A Potential | ||||||
Sequences
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References
| [1] | "The complete genome sequence of Mycobacterium bovis." Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J. Hewinson R.G.Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-935 / AF2122/97. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX248341 Genomic DNA. Translation: CAD97076.1. |
| RefSeq | NP_855872.1. NC_002945.3. |
3D structure databases | |
| ProteinModelPortal | P63855. |
| SMR | P63855. Positions 72-324. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 233413.Mb2223c. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAD97076; CAD97076; Mb2223c. |
| GeneID | 1091345. |
| KEGG | mbo:Mb2223c. |
| PATRIC | 18006586. VBIMycBov88188_2439. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1622. |
| HOGENOM | HOG000245527. |
| KO | K02275. |
| OMA | MRELWTW. |
| ProtClustDB | CLSK791696. |
Family and domain databases | |
| Gene3D | 1.10.287.90. 1 hit. 2.60.40.420. 1 hit. |
| 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. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | COX2_MYCBO | ||||||||
| Accession | Primary (citable) accession number: P63855 Secondary accession number(s): Q10375 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
