Reviewed, UniProtKB/Swiss-Prot A8LJR6 (ATPA2_DINSH)

Names and origin

Protein names

Recommended name:
    ATP synthase subunit alpha 2
    EC=3.6.3.14
Alternative name(s):
    F-ATPase subunit alpha 2
    ATP synthase F1 sector subunit alpha 2

Gene names

Name:	atpA2
Ordered Locus Names:	Dshi_2936

Organism

Dinoroseobacter shibae (strain DFL 12) [Complete proteome] [HAMAP]

Taxonomic identifier

398580 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Dinoroseobacter

Protein attributes

Sequence length	512 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit By similarity.
Catalytic activity	ATP + H2O + H+(In) = ADP + phosphate + H+(Out). HAMAP MF_01346
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 four main subunits: a1, b1, b'1 and c(9-12) By similarity.
Subcellular location	Cell inner membrane; Peripheral membrane protein By similarity.
Sequence similarities	Belongs to the ATPase alpha/beta chains family.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(1) Cell inner membrane Cell membrane Membrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	plasma membrane ATP synthesis coupled proton transport Inferred from electronic annotation. Source: HAMAP
Cellular component	extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW proton-transporting ATP synthase complex, catalytic core F(1) Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP hydrogen ion transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: HAMAP proton-transporting ATPase activity, rotational mechanism 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 – 512	512	ATP synthase subunit alpha 2 HAMAP MF_01346		PRO_0000339032
Regions
	Nucleotide binding	169 – 176	8	ATP By similarity
Sites
	Site	372	1	Required for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	A8LJR6-1 [UniParc]. Last modified December 4, 2007. Version 1. Checksum: E67A74DAAFD387A4	FASTA	512	55,053
	10 20 30 40 50 60 MGIQAAEISA ILKEQIKNFG QEAEVAEVGR VLSVGDGIAR VHGLDNVQAG EMVEFPGGIR 70 80 90 100 110 120 GMALNLEIDN VGVVIFGSDR DIKEGDIVKR TKSIVDVPVG DALLGRVVDG LGNPLDGKGP 130 140 150 160 170 180 IETTERSIAD VKAPGIIPRK SVHEPMATGL KSVDAMIPIG RGQRELIIGD RQTGKTAVAL 190 200 210 220 230 240 DTILNQKAYN DAAGDDESKK LYCVYVAVGQ KRSTVAQLVK KLEETGAIEY SIVVAATASD 250 260 270 280 290 300 PAPMQFLAPY AATSMAEFFR DNGRHALIIY DDLSKQAVSY RQMSLLLRRP PGREAYPGDV 310 320 330 340 350 360 FYLHSRLLER SAKLGDDHGN GSLTALPIIE TQGGDVSAFI PTNVISITDG QIFLETELFY 370 380 390 400 410 420 QGIRPAVNTG LSVSRVGSSA QTNAMKSVAG PVKLELAQYR EMAAFAQFGS DLDAATQQLL 430 440 450 460 470 480 NRGARLTELM KQPQYSPLTN AEIVCVIFAG TKGYLDKIPV GDVGRYEKGL LAHLRGKHKG 490 500 510 LLDYITKEDP KIKGEAEDKI RAALDEFAAT FA

References

[1]

"Complete sequence of chromosome of Dinoroseobacter shibae DFL 12." Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L. , Kyrpides N., Kim E., Richardson P. Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000830 Genomic DNA. Translation: ABV94669.1.
RefSeq	YP_001534270.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5710787.
GenomeReviews	Gene locus Dshi_2936 in contig CP000830_GR.
KEGG	dsh:Dshi_2936.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	KQVAIIF.
Family and domain databases
HAMAP	MF_01346. [Tree]
InterPro	IPR005294. ATPase_F1-cplx_asu. IPR017458. ATPase_F1-cplx_asu_C. IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C. IPR004100. ATPase_F1/V1/A1-cplx_a/bsu_N. IPR020003. ATPase_F1/V1/A1_a/bsu_AS. IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd. [Graphical view]
PANTHER	PTHR15184:SF3. ATPase_F1_a. 1 hit.
Pfam	PF00006. ATP-synt_ab. 1 hit. PF00306. ATP-synt_ab_C. 1 hit. PF02874. ATP-synt_ab_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR00962. atpA. 1 hit.
PROSITE	PS00152. ATPASE_ALPHA_BETA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATPA2_DINSH

Accession

Primary (citable) accession number: A8LJR6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	December 4, 2007
Last modified:	November 3, 2009
This is version 17 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)