Q9B8D5 (ATP9_CANAL) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 58.
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: ATP synthase subunit 9, mitochondrial Alternative name(s): Lipid-binding protein | ||||
| Gene names |
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| Encoded on | Mitochondrion | ||||
| Organism | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) | ||||
| Taxonomic identifier | 237561 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida |
Protein attributes
| Sequence length | 76 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extramembraneous catalytic core and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F0 domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element By similarity. |
| Subunit structure | F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a, b and c. |
| Subcellular location | Mitochondrion membrane; Multi-pass membrane protein Potential. |
| Sequence similarities | Belongs to the ATPase C chain family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Hydrogen ion transport Ion transport Transport |
| Cellular component | CF(0) Membrane Mitochondrion |
| Domain | Transmembrane Transmembrane helix |
| Ligand | Lipid-binding |
| Gene Ontology (GO) | |
| Biological process | ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro ATP synthesis coupled proton transportInferred from electronic annotation. Source: InterPro |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial membraneInferred from electronic annotation. Source: UniProtKB-SubCell proton-transporting ATP synthase complex, coupling factor F(o)Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | hydrogen ion transmembrane transporter activity Inferred from electronic annotation. Source: InterPro lipid bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 76 | 76 | ATP synthase subunit 9, mitochondrial | PRO_0000356858 | |||||
Regions | |||||||||
| Transmembrane | 14 – 34 | 21 | Helical; Potential | ||||||
| Transmembrane | 52 – 72 | 21 | Helical; Potential | ||||||
Sites | |||||||||
| Site | 59 | 1 | Reversibly protonated during proton transport By similarity | ||||||
Sequences
References
| [1] | "Infrequent genetic exchange and recombination in the mitochondrial genome of Candida albicans." Anderson J.B., Wickens C., Khan M., Cowen L.E., Federspiel N.A., Jones T., Kohn L.M. J. Bacteriol. 183:865-872(2001) [PubMed: 11208783] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SC5314 / ATCC MYA-2876. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF285261 Genomic DNA. Translation: AAG59591.1. |
| RefSeq | NP_075034.1. NC_002653.1. |
3D structure databases | |
| ProteinModelPortal | Q9B8D5. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q9B8D5. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 802561. |
| KEGG | cal:CaalfMp05. |
Organism-specific databases | |
| CGD | CAF0007370. ATP9. |
Phylogenomic databases | |
| HOGENOM | HBG753983. |
| PhylomeDB | Q9B8D5. |
Family and domain databases | |
| InterPro | IPR000454. ATPase_F0-cplx_csu. IPR020537. ATPase_F0-cplx_csu_DDCD_BS. IPR002379. ATPase_F0/V0-cplx_csu. [Graphical view] |
| Gene3D | G3DSA:1.20.20.10. ATPase_F0/V0_c. 1 hit. |
| KO | K02128. |
| Pfam | PF00137. ATP-synt_C. 1 hit. [Graphical view] |
| PRINTS | PR00124. ATPASEC. |
| SUPFAM | SSF81333. ATPase_F0/V0_c. 1 hit. |
| PROSITE | PS00605. ATPASE_C. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ATP9_CANAL | ||||||||
| Accession | Primary (citable) accession number: Q9B8D5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| Candida albicans Candida albicans: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

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