Reviewed, UniProtKB/Swiss-Prot Q8G2E1 (ATP6_BRUSU)

Names and origin

Protein names

Recommended name:
    ATP synthase subunit a
Alternative name(s):
    F-ATPase subunit 6
    ATP synthase F0 sector subunit a

Gene names

Name:	atpB
Ordered Locus Names:	BR0382

Organism

Brucella suis [Complete proteome] [HAMAP]

Taxonomic identifier

29461 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length	249 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane By similarity.
Subunit structure	F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a1, b2 and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF1 is attached to CF0 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.
Sequence similarities	Belongs to the ATPase A 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
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-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW proton-transporting ATP synthase complex, coupling factor F(o) Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	hydrogen ion 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 – 249	249	ATP synthase subunit a HAMAP MF_01393		PRO_0000362258
Regions
	Transmembrane	26 – 46	21	Potential
	Transmembrane	84 – 104	21	Potential
	Transmembrane	114 – 134	21	Potential
	Transmembrane	143 – 163	21	Potential
	Transmembrane	185 – 205	21	Potential
	Transmembrane	208 – 228	21	Potential

Sequences

	Sequence		Length	Mass (Da)
	Q8G2E1-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 0322177F778BAE6D	FASTA	249	26,979
	10 20 30 40 50 60 MANDPIHQFQ VSRWIPIDVG GVDLSFTNVS AFMVATVVLA SGFLYLTSSG RGLIPTRLQS 70 80 90 100 110 120 VSEMAYEFVA TSLRDSAGSK GMKFFPFVFS LFMFVLVANF IGLFPYFYTV TSQIIVTFAL 130 140 150 160 170 180 SLLVIGTVIF YGFFKHGFGF LKLFVPSGVP GIIVPLVVLI EIISFLSRPI SLSVRLFANM 190 200 210 220 230 240 LAGHITLKVF AGFVVSLSSL GALGIGGAVL PLLMTVAITA LEFLVAFLQA YVFTVLTCMY INDAVHPGH

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 / Biovar 1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014291 Genomic DNA. Translation: AAN29328.1.
RefSeq	NP_697413.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1166043.
GenomeReviews	Gene locus BR0382 in contig AE014291_GR.
KEGG	bms:BR0382.
TIGR	BR0382.
Phylogenomic databases
HOGENOM	Q8G2E1.
OMA	MDQFIVK
Enzyme and pathway databases
BioCyc	BSUI204722:BR_0382-MON.
Family and domain databases
HAMAP	MF_01393. [Tree]
InterPro	IPR000568. ATPase_F0-cplx_asu. [Graphical view]
Gene3D	G3DSA:1.20.120.220. ATPase_F0_A. 1 hit.
PANTHER	PTHR11410. ATPase_F0_A. 1 hit.
Pfam	PF00119. ATP-synt_A. 1 hit. [Graphical view]
PRINTS	PR00123. ATPASEA.
TIGRFAMs	TIGR01131. ATP_synt_6_or_A. 1 hit.
PROSITE	PS00449. ATPASE_A. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATP6_BRUSU

Accession

Primary (citable) accession number: Q8G2E1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	March 1, 2003
Last modified:	November 24, 2009
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)