Q184E7 (VATA_CLOD6) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 55.
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: V-type ATP synthase alpha chain EC=3.6.3.14 Alternative name(s): V-ATPase subunit A | ||||
| Gene names |
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| Organism | Clostridium difficile (strain 630) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 272563 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Clostridia › Clostridiales › Peptostreptococcaceae › ![]() |
Protein attributes
| Sequence length | 592 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type alpha chain is a catalytic subunit By similarity. HAMAP-Rule MF_00309 |
| Catalytic activity | ATP + H2O + H+(In) = ADP + phosphate + H+(Out). HAMAP-Rule MF_00309 |
| Sequence similarities | Belongs to the ATPase alpha/beta chains family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | ATP synthesis Hydrogen ion transport Ion transport Transport |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Hydrolase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro plasma membrane ATP synthesis coupled proton transportInferred from electronic annotation. Source: HAMAP |
| Cellular_component | proton-transporting two-sector ATPase complex, catalytic domain Inferred from electronic annotation. Source: InterPro |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: HAMAP proton-transporting ATP synthase activity, rotational mechanismInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 592 | 592 | V-type ATP synthase alpha chain HAMAP-Rule MF_00309 | PRO_0000322463 | |||||
Regions | |||||||||
| Nucleotide binding | 232 – 239 | 8 | ATP Potential | ||||||
Sequences
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References
| [1] | "The multidrug-resistant human pathogen Clostridium difficile has a highly mobile, mosaic genome." Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N., Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H., Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N., Brooks K., Chillingworth T. Parkhill J.Nat. Genet. 38:779-786(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 630. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AM180355 Genomic DNA. Translation: CAJ69848.1. |
| RefSeq | YP_001089472.1. NC_009089.1. |
3D structure databases | |
| ProteinModelPortal | Q184E7. |
| SMR | Q184E7. Positions 60-589. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 272563.CD2956. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAJ69848; CAJ69848; CD630_29560. |
| GeneID | 4913755. |
| KEGG | cdf:CD630_29560. |
| PATRIC | 19444433. VBICloDif38397_3100. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1155. |
| HOGENOM | HOG000161057. |
| KO | K02117. |
| OMA | WALDAKL. |
| ProtClustDB | PRK04192. |
Enzyme and pathway databases | |
| BioCyc | CDIF272563:GJFE-3189-MONOMER. |
Family and domain databases | |
| Gene3D | 1.10.1140.10. 1 hit. |
| HAMAP | MF_00309. ATP_synth_A_arch. |
| InterPro | IPR003593. AAA+_ATPase. IPR020003. ATPase_a/bsu_AS. IPR004100. ATPase_a/bsu_N. IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C. IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd. IPR024034. ATPase_F1_bsu/V1_C. IPR022878. V-ATPase_su_A/alpha. [Graphical view] |
| Pfam | PF00006. ATP-synt_ab. 1 hit. PF00306. ATP-synt_ab_C. 1 hit. PF02874. ATP-synt_ab_N. 1 hit. [Graphical view] |
| SMART | SM00382. AAA. 1 hit. [Graphical view] |
| SUPFAM | SSF47917. ATPase_a/b_C. 1 hit. SSF50615. ATPase_a/b_N. 1 hit. |
| PROSITE | PS00152. ATPASE_ALPHA_BETA. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | VATA_CLOD6 | ||||||||
| Accession | Primary (citable) accession number: Q184E7 | ||||||||
| 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
