Reviewed, UniProtKB/Swiss-Prot Q3B1F4 (ATPA2_PELLD)

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:	Plut_1985

Organism

Pelodictyon luteolum (strain DSM 273) (Chlorobium luteolum (strain DSM 273)) [Complete proteome] [HAMAP]

Taxonomic identifier

319225 [NCBI]

Taxonomic lineage

Bacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobium/Pelodictyon group › Pelodictyon

Protein attributes

Sequence length	526 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 – 526	526	ATP synthase subunit alpha 2 HAMAP MF_01346		PRO_0000238316
Regions
	Nucleotide binding	171 – 178	8	ATP By similarity
Sites
	Site	382	1	Required for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3B1F4-1 [UniParc]. Last modified November 22, 2005. Version 1. Checksum: CD26B2A5E3008A6B	FASTA	526	56,665
	10 20 30 40 50 60 MSTTVRPDEV SSILRKQLAG FESEAEVYDV GTVLQVGDGI ARVYGLSKAA AGELLEFPNK 70 80 90 100 110 120 VMGMALNLEE DNVGAVLFGD STEVKEGDTV KRTGILASVP VGEAMLGRVV NPLGVPIDGK 130 140 150 160 170 180 GIIDTDIRLP LERRAPGVIY RKSVHEPLQT GLKAIDSMIP IGRGQRELII GDRQTGKTAV 190 200 210 220 230 240 ALDTIINQKG KGVYCIYVAI GLKGSTVAQV VNTLEKHGAM EYTTVITATA SDPAPLQFIA 250 260 270 280 290 300 PFAGAALGEY FRDTGRHALV VYDDLSKQAV AYRQLSLLLR RPPGREAYPG DVFFLHSRLL 310 320 330 340 350 360 ERAAKITDDI EVAKKMNDLP DALRPMVQGG GSLTALPVIE TQAGDVSAYI PTNVISITDG 370 380 390 400 410 420 QIFLESNLFN SGQRPAINVG ISVSRVGGAA QIKAMKKVAG TLRLDLAQFR ELEAFSKFGS 430 440 450 460 470 480 DLDKTTKAQL DRGARLVEIL KQGQYVPMPV ERQVAIIFLG TQGLLDLVAV QHVKKFEEEF 490 500 510 520 LAMLDLKHSD ILKSIAETGA LEADVAGRLK EAAQKFVTTF NDKVKA

References

[1]

"Complete sequence of Pelodictyon luteolum DSM 273." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P. Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000096 Genomic DNA. Translation: ABB24827.1.
RefSeq	YP_375870.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q3B1F4.
Genome annotation databases
GeneID	3744954.
GenomeReviews	Gene locus Plut_1985 in contig CP000096_GR.
KEGG	plt:Plut_1985.
NMPDR	fig|319225.3.peg.1965.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q3B1F4.
OMA	KQVAIIF.
Enzyme and pathway databases
BioCyc	PLUT319225:PLUT_1985-MON.
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_PELLD

Accession

Primary (citable) accession number: Q3B1F4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	November 22, 2005
Last modified:	November 3, 2009
This is version 35 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)