Q8G2E1 (ATP6_BRUSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP synthase subunit a

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

Gene names

Name:	atpB
Ordered Locus Names:	BR0382, BS1330_I0383

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	249 AA.
Sequence status	Complete.
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. HAMAP MF_01393
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 HAMAP MF_01393.
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 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 – 249	249	ATP synthase subunit a HAMAP MF_01393		PRO_0000362258
Regions
	Transmembrane	26 – 46	21	Helical; Potential
	Transmembrane	84 – 104	21	Helical; Potential
	Transmembrane	114 – 134	21	Helical; Potential
	Transmembrane	143 – 163	21	Helical; Potential
	Transmembrane	185 – 205	21	Helical; Potential
	Transmembrane	208 – 228	21	Helical; Potential

Sequences

	Sequence		Length	Mass (Da)
	Q8G2E1 [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.

[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: AAN29328.1. CP002997 Genomic DNA. Translation: AEM17741.1.
RefSeq	NP_697413.1. NC_004310.3.
3D structure databases
ProteinModelPortal	Q8G2E1.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1166043.
GenomeReviews	Gene locus BR0382 in contig AE014291_GR.
KEGG	bms:BR0382.
PATRIC	17789060. VBIBruSui107850_0398.
TIGR	BR0382.
Phylogenomic databases
HOGENOM	HBG734175.
OMA	TFILVAN.
PhylomeDB	Q8G2E1.
ProtClustDB	PRK05815.
Enzyme and pathway databases
BioCyc	BSUI204722:BR_0382-MONOMER.
Family and domain databases
HAMAP	MF_01393. ATP_synth_a_bact. [Tree]
InterPro	IPR000568. ATPase_F0-cplx_asu. IPR023011. ATPase_F0-cplx_asu_AS. [Graphical view]
Gene3D	G3DSA:1.20.120.220. ATPase_F0_A. 1 hit.
KO	K02108.
PANTHER	PTHR11410. ATPase_F0_A. 1 hit.
Pfam	PF00119. ATP-synt_A. 1 hit. [Graphical view]
PRINTS	PR00123. ATPASEA.
SUPFAM	SSF81336. ATPase_F0_A. 1 hit.
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
Secondary accession number(s): G0K6K4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	March 1, 2003
Last modified:	January 25, 2012
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program