Q4UNH9 (ATPL_RICFE) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 50.
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 c Alternative name(s): ATP synthase F(0) sector subunit c F-type ATPase subunit c Short name=F-ATPase subunit c Lipid-binding protein | ||||
| Gene names |
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| Organism | Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 315456 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › spotted fever group |
Protein attributes
| Sequence length | 74 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_01396 Key component of the F0 channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F1 delta and epsilon subunits By similarity. HAMAP MF_01396 |
| 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; Multi-pass membrane protein By similarity HAMAP MF_01396. |
| Sequence similarities | Belongs to the ATPase C 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 |
| Ligand | Lipid-binding |
| Technical term | Complete proteome |
| 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 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 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 – 74 | 74 | ATP synthase subunit c HAMAP MF_01396 | PRO_0000288729 | |||||
Regions | |||||||||
| Transmembrane | 8 – 28 | 21 | Helical; Potential | ||||||
| Transmembrane | 52 – 72 | 21 | Helical; Potential | ||||||
Sites | |||||||||
| Site | 58 | 1 | Reversibly protonated during proton transport By similarity | ||||||
Sequences
References
| [1] | "The genome sequence of Rickettsia felis identifies the first putative conjugative plasmid in an obligate intracellular parasite." Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E., Parinello H., Claverie J.-M., Raoult D. PLoS Biol. 3:1-12(2005) [PubMed: 15984913] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC VR-1525 / URRWXCal2. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000053 Genomic DNA. Translation: AAY60880.1. |
| RefSeq | YP_246045.1. NC_007109.1. |
3D structure databases | |
| ProteinModelPortal | Q4UNH9. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 3401255. |
| GenomeReviews | Gene locus RF_0029 in contig CP000053_GR. |
| KEGG | rfe:RF_0029. |
| NMPDR | fig|315456.3.peg.511. |
| PATRIC | 17890382. VBIRicFel64634_0036. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG753983. |
| OMA | FMAIGMY. |
| ProtClustDB | PRK07558. |
Enzyme and pathway databases | |
| BioCyc | RFEL315456:RF_0029-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01396. ATP_synth_c_bact. [Tree] |
| 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 | K02110. |
| 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 | ATPL_RICFE | ||||||||
| Accession | Primary (citable) accession number: Q4UNH9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Rickettsia felis (Rickettsia azadi) Rickettsia felis (strain URRWXCal2): entries and gene names |
| SIMILARITY comments Index of protein domains and families |

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