B4RJF6 (ATPF_NEIG2) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
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 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 | Neisseria gonorrhoeae (strain NCCP11945) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 521006 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria › ![]() |
Protein attributes
| Sequence length | 156 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 – 156 | 156 | ATP synthase subunit b HAMAP-Rule MF_01398 | PRO_0000368620 | |||||
Regions | |||||||||
| Transmembrane | 7 – 27 | 21 | Helical; Potential | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Complete genome sequence of Neisseria gonorrhoeae NCCP11945." Chung G.T., Yoo J.S., Oh H.B., Lee Y.S., Cha S.H., Kim S.J., Yoo C.K. J. Bacteriol. 190:6035-6036(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCCP11945. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP001050 Genomic DNA. Translation: ACF31221.1. |
| RefSeq | YP_002003247.1. NC_011035.1. |
3D structure databases | |
| ProteinModelPortal | B4RJF6. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 521006.NGK_2622. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ACF31221; ACF31221; NGK_2622. |
| GeneID | 6448057. |
| KEGG | ngk:NGK_2622. |
| PATRIC | 20344023. VBINeiGon87511_2839. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0711. |
| HOGENOM | HOG000015378. |
| KO | K02109. |
| OMA | NPGLIFW. |
| ProtClustDB | PRK05759. |
Enzyme and pathway databases | |
| BioCyc | NGON521006:GJ73-2695-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01398. ATP_synth_b_bact. |
| InterPro | IPR002146. ATPase_F0-cplx_b/b'su_bac. IPR005864. ATPase_F0-cplx_bsu_bac. [Graphical view] |
| Pfam | PF00430. ATP-synt_B. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01144. ATP_synt_b. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ATPF_NEIG2 | ||||||||
| Accession | Primary (citable) accession number: B4RJF6 | ||||||||
| 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
