Q1RGZ0 (ATPF_RICBR) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 43.
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 Alternative name(s): ATP synthase F(0) sector subunit b ATPase subunit I F-type ATPase subunit b Short name=F-ATPase subunit b | ||||
| Gene names |
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| Organism | Rickettsia bellii (strain RML369-C) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 336407 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › belli group › ![]() |
Protein attributes
| Sequence length | 157 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_01398 Component of the F0 channel, it forms part of the peripheral stalk, linking F1 to F0 By similarity. HAMAP-Rule 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-Rule 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 | plasma membrane ATP synthesis coupled proton transport Inferred from electronic annotation. Source: HAMAP |
| 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 | 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 – 157 | 157 | ATP synthase subunit b HAMAP-Rule MF_01398 | PRO_0000288722 | ||||
Regions | ||||||||
| Transmembrane | 1 – 21 | 21 | Helical; Potential | |||||
Sequences
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References
| [1] | "Genome sequence of Rickettsia bellii illuminates the role of amoebae in gene exchanges between intracellular pathogens." Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C., Fournier P.-E., Claverie J.-M., Raoult D. PLoS Genet. 2:733-744(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RML369-C. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000087 Genomic DNA. Translation: ABE05374.1. |
| RefSeq | YP_538463.1. NC_007940.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 336407.RBE_1293. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABE05374; ABE05374; RBE_1293. |
| GeneID | 3995982. |
| KEGG | rbe:RBE_1293. |
| PATRIC | 17884218. VBIRicBel102610_1457. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0711. |
| HOGENOM | HOG000010613. |
| KO | K02109. |
| OMA | AIQLIQN. |
| ProtClustDB | PRK06568. |
Enzyme and pathway databases | |
| BioCyc | RBEL336407:GJCY-1331-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01398. ATP_synth_b_bact. |
| 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 | ATPF_RICBR | ||||||||
| Accession | Primary (citable) accession number: Q1RGZ0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Rickettsia bellii strain RML369-C Rickettsia bellii (strain RML369-C): entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with
