Q8G2D8 (ATPF2_BRUSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP synthase subunit b 2

Alternative name(s):
ATP synthase F(0) sector subunit b 2
ATPase subunit I 2
F-type ATPase subunit b 2
Short name=F-ATPase subunit b 2

Gene names

Name:	atpF2
Synonyms:	atpF
Ordered Locus Names:	BR0385, BS1330_I0386

Organism

Brucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]

Taxonomic identifier

204722 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length	159 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 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 – 159	159	ATP synthase subunit b 2 HAMAP MF_01398		PRO_0000368375
Regions
	Transmembrane	1 – 21	21	Helical; Potential

Sequences

	Sequence		Length	Mass (Da)
	Q8G2D8 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 55D136A2EAFD34FB	FASTA	159	17,522
	10 20 30 40 50 60 MDATFWAFIA LVIFVVIVVY MKVPGMIGRT LDERADRIKK ELEEARTLRE EAQQLLAEYH 70 80 90 100 110 120 RKRKEAEKEA GDIVASAERE AKALLEEAKR ATEEYVARRN KLAEQKIATA ETDAINAVRA 130 140 150 SAVDLAVAAA GSILAEKVDA KAAGNLFNDA LAQVKSHLN

References

[1]

"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts." Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed: 12271122] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

[2]

"Revised genome sequence of Brucella suis 1330." Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R. J. Bacteriol. 193:6410-6410(2011) [PubMed: 22038969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014291 Genomic DNA. Translation: AAN29331.1. CP002997 Genomic DNA. Translation: AEM17744.1.
RefSeq	NP_697416.1. NC_004310.3.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1166046.
GenomeReviews	Gene locus BR0385 in contig AE014291_GR.
KEGG	bms:BR0385.
PATRIC	17789066. VBIBruSui107850_0401.
TIGR	BR0385.
Phylogenomic databases
HOGENOM	HBG692690.
OMA	AKMEDFV.
ProtClustDB	PRK09173.
Enzyme and pathway databases
BioCyc	BSUI204722:BR_0385-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

ATPF2_BRUSU

Accession

Primary (citable) accession number: Q8G2D8
Secondary accession number(s): G0K6K7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	March 1, 2003
Last modified:	January 25, 2012
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program