Reviewed, UniProtKB/Swiss-Prot A1UY41 (ATPA2_BURMS)

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:	BMASAVP1_1297

Organism

Burkholderia mallei (strain SAVP1) [Complete proteome] [HAMAP]

Taxonomic identifier

320388 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length	670 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 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; 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 – 670	670	ATP synthase subunit alpha 2 HAMAP MF_01346		PRO_0000339022
Regions
	Nucleotide binding	180 – 187	8	ATP By similarity
Sites
	Site	373	1	Required for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1UY41-1 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: 76A50643D8FB0FC8	FASTA	670	70,296
	10 20 30 40 50 60 MTPTPDAPAA ADAATGAGWL ARRRGALARV ALAPIAQAIG RVERVADGIA FVSGLEDTML 70 80 90 100 110 120 NEVLRFEGGV TGFAHTLDED LISVVLLDPD AGVRAQTAVA RTGAVLEVPA GPQLLGRVVD 130 140 150 160 170 180 PLGRPLDGGA PLDAAHTLPI ERAAPAIIER DLVSEPLDTG VLIVDALFTI GRGQRELIIG 190 200 210 220 230 240 DRATGKTSLA IDAIVNQRHS DVICVYVAIG QRASAVRRVI DAVRRYGAPE RCVFVVAPAA 250 260 270 280 290 300 CAPGLQWIAP FAGFSIAEYF RDRGQHALVV VDDLTKHAAT HRELALLTRE PPGREAYPGD 310 320 330 340 350 360 IFYVHARLLE RAAKLSAALG GGSLSALPIA ETDAGNLAAY IPTNLISITD GQIVLDSALF 370 380 390 400 410 420 AANQRPAVDV GLSVSRVGGK AQHPALRAAS GRLRLDYAQF LELEAFTRFG GLTDARLRAQ 430 440 450 460 470 480 ITRGERIRAL ITQPRFRALR TLDEVVLLKA LAAGTLDAMS PDLVAPLRER LPAWLDARIA 490 500 510 520 530 540 ALTPALAPPR DWLADDAALD ALAESVGELI ERIAADAARR ATAGMPAEDA AGDIGGAFGG 550 560 570 580 590 600 EQARGDADRD ADHGANREVS REVSPEASRE VSREVSREVS HEADRDAAAD AARVAGRAPG 610 620 630 640 650 660 RAEPDRAVPR AMPDGPPRAQ ADGDRASASR PPPDARGDAA RTAPSPQGGA DANVNADANV 670 DAEAEARHKR

References

[1]	DeShazer D., Woods D.E., Nierman W.C. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000525 Genomic DNA. Translation: ABM47788.1.
RefSeq	YP_990894.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4678427.
GenomeReviews	Gene locus BMASAVP1_1297 in contig CP000525_GR.
KEGG	bmv:BMASAVP1_1297.
TIGR	BMASAVP1_1297.
Phylogenomic databases
OMA	NVLCVYC.
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_BURMS

Accession

Primary (citable) accession number: A1UY41

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	February 6, 2007
Last modified:	November 3, 2009
This is version 25 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)