Reviewed, UniProtKB/Swiss-Prot A1V8T3 (ATPA1_BURMS)

Names and origin

Protein names

Recommended name:
    ATP synthase subunit alpha 1
    EC=3.6.3.14
Alternative name(s):
    F-ATPase subunit alpha 1
    ATP synthase F1 sector subunit alpha 1

Gene names

Name:	atpA1
Ordered Locus Names:	BMASAVP1_A3357

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	513 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 – 513	513	ATP synthase subunit alpha 1 HAMAP MF_01346		PRO_0000339021
Regions
	Nucleotide binding	169 – 176	8	ATP By similarity
Sites
	Site	373	1	Required for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1V8T3-1 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: CE603CEBB6B09ADB	FASTA	513	55,926
	10 20 30 40 50 60 MQLNPSEISE LIKSRIQGLE ASADVRNQGT VISVTDGIVR IHGLSDVMQG EMLEFPGNTF 70 80 90 100 110 120 GLALNLERDS VGAVILGEYE HISEGDIVKT TGRILEVPVG PELVGRVLDA LGNPIDGKGP 130 140 150 160 170 180 VNAKLTDAIE KIAPGVIWRK SVSQPVQTGL KSIDSMVPIG RGQRELIIGD RQCGKTAVAI 190 200 210 220 230 240 DTIINQKGKD LICIYVAIGQ KASSIMNVVR KLEETGALEY TIVVAASASE SAAMQYLAPY 250 260 270 280 290 300 AGCTMGEYFR DRGQDALIIY DDLTKQAWAY RQISLLLRRP PGREAYPGDV FYLHSRLLER 310 320 330 340 350 360 AARVSEEYVE KFTNGEVKGK SGSLTALPVI ETQAGDVTAF VPTNVISITD GQIFLETDLF 370 380 390 400 410 420 NAGIRPAINA GVSVSRVGGA AQTKVVKKLS GGIRTDLAQY RELAAFAQFA SDLDEATRKQ 430 440 450 460 470 480 LERGRRVTEL LKQPQYQPLQ VWELAVSLFS ANNGYLDDLD VKDVLPFEKG LREYLKTSHA 490 500 510 DLIKRIEDTK DLSKDDESAL HAALKDFKKS GAY

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	CP000526 Genomic DNA. Translation: ABM51897.1.
RefSeq	YP_994636.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4679018.
GenomeReviews	Gene locus BMASAVP1_A3357 in contig CP000526_GR.
KEGG	bmv:BMASAVP1_A3357.
TIGR	BMASAVP1_A3357.
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

ATPA1_BURMS

Accession

Primary (citable) accession number: A1V8T3

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)