Q2YLI4 (ATPD_BRUA2) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 49.
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 delta Alternative name(s): ATP synthase F(1) sector subunit delta F-type ATPase subunit delta Short name=F-ATPase subunit delta | ||||
| Gene names |
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| Organism | Brucella abortus (strain 2308) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 359391 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › ![]() |
Protein attributes
| Sequence length | 186 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | F1F0 ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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 By similarity. HAMAP-Rule MF_01416 This protein is part of the stalk that links CF0 to CF1. It either transmits conformational changes from CF0 to CF1 or is implicated in proton conduction By similarity. HAMAP-Rule MF_01416 |
| Subunit structure | F-type ATPases have 2 components, F1 - the catalytic core - and F0 - the membrane proton channel. F1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. F0 has three main subunits: a1, b2 and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F1 is attached to F0 by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains By similarity. |
| Subcellular location | Cell inner membrane; Peripheral membrane protein By similarity HAMAP-Rule MF_01416. |
| Sequence similarities | Belongs to the ATPase delta chain family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | ATP synthesis Hydrogen ion transport Ion transport Transport |
| Cellular component | CF(1) Cell inner membrane Cell membrane Membrane |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | plasma membrane ATP synthesis coupled proton transport Inferred from electronic annotation. Source: HAMAP |
| Cellular_component | plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell proton-transporting ATP synthase complex, catalytic core F(1)Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | proton-transporting ATP synthase activity, rotational mechanism Inferred 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 – 186 | 186 | ATP synthase subunit delta HAMAP-Rule MF_01416 | PRO_0000370909 | |||
Sequences
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References
| [1] | "Whole-genome analyses of speciation events in pathogenic Brucellae." Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E. Infect. Immun. 73:8353-8361(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 2308. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AM040264 Genomic DNA. Translation: CAJ11766.1. |
| RefSeq | YP_415156.1. NC_007618.1. |
3D structure databases | |
| ProteinModelPortal | Q2YLI4. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 359391.BAB1_1810. |
Proteomic databases | |
| PRIDE | Q2YLI4. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAJ11766; CAJ11766; BAB1_1810. |
| GeneID | 3788633. |
| KEGG | bmf:BAB1_1810. |
| PATRIC | 17846654. VBIBruMel86222_1876. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0712. |
| HOGENOM | HOG000075825. |
| KO | K02113. |
| OMA | ARNRRLF. |
| ProtClustDB | PRK05758. |
Enzyme and pathway databases | |
| BioCyc | BMEL359391:GJOQ-1854-MONOMER. |
Family and domain databases | |
| Gene3D | 1.10.520.20. 1 hit. |
| HAMAP | MF_01416. ATP_synth_delta_bact. |
| InterPro | IPR000711. ATPase_F1-cplx_OSCP/dsu. IPR020781. ATPase_F1-cplx_OSCP/dsu_CS. IPR026015. ATPase_OSCP/delta_N. [Graphical view] |
| PANTHER | PTHR11910. PTHR11910. 1 hit. |
| Pfam | PF00213. OSCP. 1 hit. [Graphical view] |
| PRINTS | PR00125. ATPASEDELTA. |
| SUPFAM | SSF47928. ATPsynt_OSCP. 1 hit. |
| TIGRFAMs | TIGR01145. ATP_synt_delta. 1 hit. |
| PROSITE | PS00389. ATPASE_DELTA. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ATPD_BRUA2 | ||||||||
| Accession | Primary (citable) accession number: Q2YLI4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Brucella abortus strain 2308 Brucella abortus (strain 2308): entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with
