Q8E5V2 (ATPF_STRA3) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 54.
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 |
| ||||
| Organism | Streptococcus agalactiae serotype III [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 216495 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus |
Protein attributes
| Sequence length | 165 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 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 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 – 165 | 165 | ATP synthase subunit b HAMAP MF_01398 | PRO_0000368793 | |||||
Regions | |||||||||
| Transmembrane | 7 – 27 | 21 | Helical; Potential | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive neonatal disease." Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T., Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F. Mol. Microbiol. 45:1499-1513(2002) [PubMed: 12354221] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NEM316 / Serotype III. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AL766847 Genomic DNA. Translation: CAD46521.1. |
| RefSeq | NP_735327.1. NC_004368.1. |
3D structure databases | |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBSTRT00000002546; EBSTRP00000002464; EBSTRG00000002546. |
| GeneID | 1029857. |
| GenomeReviews | Gene locus gbs0877 in contig AL732656_GR. |
| KEGG | san:gbs0877. |
| PATRIC | 19637616. VBIStrAga3577_0900. |
Organism-specific databases | |
| GenoList | gbs0877. |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000027998. |
| HOGENOM | HBG617328. |
| OMA | LEKYNAQ. |
| ProtClustDB | PRK05759. |
Enzyme and pathway databases | |
| BioCyc | SAGA211110:GBS0877-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01398. ATP_synth_b_bact. [Tree] |
| InterPro | IPR002146. ATPase_F0-cplx_b/b'su_bac. IPR005864. ATPase_F0-cplx_bsu_bac. [Graphical view] |
| KO | K02109. |
| Pfam | PF00430. ATP-synt_B. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01144. ATP_synt_b. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ATPF_STRA3 | ||||||||
| Accession | Primary (citable) accession number: Q8E5V2 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with