A9IQI8 (ATPF2_BART1) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 29.
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 b 2 Alternative name(s): ATP synthase F(0) sector subunit b 2 ATPase subunit I 2 F-type ATPase subunit b 2 Short name=F-ATPase subunit b 2 | ||||
| Gene names |
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| Organism | Bartonella tribocorum (strain CIP 105476 / IBS 506) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 382640 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella |
Protein attributes
| Sequence length | 164 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 MF_01398 Component of the F0 channel, it forms part of the peripheral stalk, linking F1 to F0 By similarity. HAMAP MF_01398 |
| 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; Single-pass membrane protein By similarity HAMAP MF_01398. |
| Sequence similarities | Belongs to the ATPase B chain family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | ATP synthesis Hydrogen ion transport Ion transport Transport |
| Cellular component | CF(0) Cell inner membrane Cell membrane Membrane |
| Domain | Transmembrane Transmembrane helix |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | ATP synthesis coupled proton transport Inferred from electronic annotation. Source: InterPro |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma 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 |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 164 | 164 | ATP synthase subunit b 2 HAMAP MF_01398 | PRO_0000368347 | |||||
Regions | |||||||||
| Transmembrane | 4 – 24 | 21 | Helical; Potential | ||||||
Sequences
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References
| [1] | "Genomic analysis of Bartonella identifies type IV secretion systems as host adaptability factors." Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G., Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C. Nat. Genet. 39:1469-1476(2007) [PubMed: 18037886] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CIP 105476 / IBS 506. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AM260525 Genomic DNA. Translation: CAK01063.1. |
| RefSeq | YP_001609058.1. NC_010161.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A9IQI8. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 5829825. |
| GenomeReviews | Gene locus BT_0625 in contig AM260525_GR. |
| PATRIC | 20549006. VBIBarTri113218_0662. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG692690. |
| OMA | AKMEDFV. |
| ProtClustDB | PRK09173. |
Enzyme and pathway databases | |
| BioCyc | BTRI382640:BT_0625-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01398. ATP_synth_b_bact. [Tree] |
| InterPro | IPR002146. ATPase_F0-cplx_b/b'su_bac. [Graphical view] |
| Pfam | PF00430. ATP-synt_B. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ATPF2_BART1 | ||||||||
| Accession | Primary (citable) accession number: A9IQI8 | ||||||||
| 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 |

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