Reviewed, UniProtKB/Swiss-Prot Q13SQ0 (ATPA2_BURXL)

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:	Bxeno_A4351
ORF Names:	Bxe_A0038

Organism

Burkholderia xenovorans (strain LB400) [Complete proteome] [HAMAP]

Taxonomic identifier

266265 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia

Protein attributes

Sequence length	513 AA.
Sequence status	Complete.
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. HAMAP MF_01346
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. HAMAP MF_01346
Subcellular location	Cell inner membrane; Peripheral membrane protein By similarity HAMAP MF_01346.
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 2 HAMAP MF_01346		PRO_0000256084
Regions
	Nucleotide binding	169 – 176	8	ATP By similarity
Sites
	Site	373	1	Required for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q13SQ0-1 [UniParc]. Last modified August 22, 2006. Version 1. Checksum: 763C5136CD1BC3A7	FASTA	513	55,938
	10 20 30 40 50 60 MQLNPSEISE LIKSRIQGLE ASADVRNQGT VISVTDGIVR IHGLSEVMQG EMLEFPGNTF 70 80 90 100 110 120 GLALNLERDS VGAVILGEYE HISEGDVVKT TGRILEVPVG PELLGRVVDA LGNPIDGKGP 130 140 150 160 170 180 INAKKTDAIE KIAPGVIWRK SVSEPVQTGL KSIDAMVPVG RGQRELIIGD RQCGKTAVAV 190 200 210 220 230 240 DTIINQKGKN LFCIYVAIGQ KASSIMNVVR KLEETGALEY TIVVAASASE SAAMQYLAPY 250 260 270 280 290 300 AGCTMGEYFR DRGQDALIVY DDLTKQAWAY RQISLLLRRP PGREAYPGDV FYLHSRLLER 310 320 330 340 350 360 AARVSEDYVE 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 VWELAVALFA ANNGYLDDLE VAQVLPFEKG LRDYLKSKHA 490 500 510 DLIKRIEDTK ELSKDDEALL HTALKDFKKS GAY

References

[1]

"Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome shaped for versatility." Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L., Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J., Parnell J.J. , Ramette A., Richardson P., Seeger M., Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M. Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006) [PubMed: 17030797] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000270 Genomic DNA. Translation: ABE32889.1.
RefSeq	YP_560941.1.
3D structure databases
SMR	Q13SQ0. Positions 29-509.
ModBase	Search...
Genome annotation databases
GeneID	4006389.
GenomeReviews	Gene locus Bxeno_A4351 in contig CP000270_GR.
KEGG	bxe:Bxe_A0038.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG565875.
OMA	GSDRDIK.
Family and domain databases
HAMAP	MF_01346. ATP_synth_alpha_bact. [Tree]
InterPro	IPR005294. ATPase_F1-cplx_asu. IPR017458. ATPase_F1-cplx_asu_C. IPR018118. ATPase_F1/A1-cplx_a/bsu_N. 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_BURXL

Accession

Primary (citable) accession number: Q13SQ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	August 22, 2006
Last modified:	February 9, 2010
This is version 31 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)