A0JY70 (ATP6_ARTS2) 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:	Arth_2611

Organism

Arthrobacter sp. (strain FB24) [Complete proteome] [HAMAP]

Taxonomic identifier

290399 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Arthrobacter

Protein attributes

Sequence length	266 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-Rule 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 membrane; Multi-pass membrane protein By similarity HAMAP-Rule 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 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 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	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 – 266	266	ATP synthase subunit a HAMAP-Rule MF_01393		PRO_1000145256
Regions
	Transmembrane	38 – 58	21	Helical; Potential
	Transmembrane	99 – 119	21	Helical; Potential
	Transmembrane	126 – 146	21	Helical; Potential
	Transmembrane	162 – 182	21	Helical; Potential
	Transmembrane	191 – 211	21	Helical; Potential
	Transmembrane	224 – 244	21	Helical; Potential

Sequences

	Sequence		Length	Mass (Da)
	A0JY70 [UniParc]. Last modified December 12, 2006. Version 1. Checksum: 2652EABD2A2005A2	FASTA	266	28,891
	10 20 30 40 50 60 MIALALPAQD SGEFNPPGIE EMHLPAILPW GAADGFSKQM LLVILSVVII ATFFLLAARK 70 80 90 100 110 120 QQLVPGKLQF AGEAAYGFVR NSIAKDIIGG KDFMKYVPLL FSLFFFILVN NIYGAIPLIQ 130 140 150 160 170 180 LPSFSHVGGA YVLAAIVYLT WIAIGVKKNG IKYFKLATVP TGVPVYILPI VIPIEIISNF 190 200 210 220 230 240 LVRPVTHSLR LFATMLAGHL IVMIAGSGIE YLVMQENILL KGTSVLVLVG AIAMYMLEAL 250 260 IMALQAYVFT LLTAIYIEGA LHADSH

References

[1]

"Complete sequence of chromosome 1 of Arthrobacter sp. FB24." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Thompson S., Brettin T., Bruce D., Han C., Tapia R., Gilna P. , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Beasley F., Chen W., Jerke K., Nakatsu C.H., Richardson P. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FB24.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000454 Genomic DNA. Translation: ABK03990.1.
RefSeq	YP_832090.1. NC_008541.1.
3D structure databases
ProteinModelPortal	A0JY70.
ModBase	Search...
Protein-protein interaction databases
STRING	290399.Arth_2611.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABK03990; ABK03990; Arth_2611.
GeneID	4444852.
KEGG	art:Arth_2611.
PATRIC	21000607. VBIArtSp72239_2990.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0356.
HOGENOM	HOG000253873.
KO	K02108.
OMA	TVTSHIV.
ProtClustDB	PRK05815.
Enzyme and pathway databases
BioCyc	ASP290399:GHIF-2663-MONOMER.
Family and domain databases
Gene3D	1.20.120.220. 1 hit.
HAMAP	MF_01393. ATP_synth_a_bact.
InterPro	IPR000568. ATPase_F0-cplx_asu. [Graphical view]
PANTHER	PTHR11410. PTHR11410. 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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATP6_ARTS2

Accession

Primary (citable) accession number: A0JY70

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	December 12, 2006
Last modified:	May 1, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program