A4Z2B7 (ATPF_BRASO) Reviewed, UniProtKB/Swiss-Prot

Names 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

Name:	atpF
Ordered Locus Names:	BRADO6689

Organism

Bradyrhizobium sp. (strain ORS278) [Complete proteome] [HAMAP]

Taxonomic identifier

114615 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Bradyrhizobium

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 four main subunits: a1, b1, b'1 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, b 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 membrane Inferred 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 HAMAP MF_01398		PRO_0000368363
Regions
	Transmembrane	8 – 28	21	Helical; Potential

Sequences

	Sequence		Length	Mass (Da)
	A4Z2B7 [UniParc]. Last modified May 29, 2007. Version 1. Checksum: FB5523332E49939E	FASTA	164	17,639
	10 20 30 40 50 60 MMHLLADPET WVAIAFVILM GLFAYLGVHR MVLKALDHRA DRIRDELAEA KRLKDEAAKV 70 80 90 100 110 120 LADYKTRRAS AEREAEEIVT SAKAEAERIA ADAKAKMEDF VARRTKAAES KIALAEAQAL 130 140 150 160 ADVRAAAAEA AVQAAATVLS QSVKGGLGDD LVAKGIAEVS RKLN

References

[1]

"Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia." Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C., Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L., Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z. , Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.-S., Saunders E., Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G., Emerich D., Vermeglio A., Medigue C., Sadowsky M. Science 316:1307-1312(2007) [PubMed: 17540897] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ORS278.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU234118 Genomic DNA. Translation: CAL80293.1.
RefSeq	YP_001208508.1. NC_009445.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A4Z2B7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5115132.
GenomeReviews	Gene locus BRADO6689 in contig CU234118_GR.
KEGG	bra:BRADO6689.
PATRIC	21229235. VBIBraSp122330_6403.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0711.
HOGENOM	HBG692690.
OMA	AKMEDFV.
ProtClustDB	CLSK818463.
Enzyme and pathway databases
BioCyc	BSP376:BRADO6689-MONOMER.
Family and domain databases
HAMAP	MF_01398. ATP_synth_b_bact. [Tree]
InterPro	IPR002146. ATPase_F0-cplx_b/b'su_bac. [Graphical view]
KO	K02109.
Pfam	PF00430. ATP-synt_B. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATPF_BRASO

Accession

Primary (citable) accession number: A4Z2B7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	May 29, 2007
Last modified:	December 14, 2011
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program