Reviewed, UniProtKB/Swiss-Prot A5III5 (ATPA2_LEGPC)

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:	LPC_3299

Organism

Legionella pneumophila (strain Corby) [Complete proteome] [HAMAP]

Taxonomic identifier

400673 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Legionellaceae › Legionella

Protein attributes

Sequence length	517 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 – 517	517	ATP synthase subunit alpha 2 HAMAP MF_01346		PRO_0000339036
Regions
	Nucleotide binding	173 – 180	8	ATP By similarity
Sites
	Site	377	1	Required for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	A5III5-1 [UniParc]. Last modified June 26, 2007. Version 1. Checksum: 50AC4FE274BF9419	FASTA	517	55,512
	10 20 30 40 50 60 MSEQVALNPS EISELIRKKI DQFSVVSEAR NEGTIVSLKD GIVRLHGLAD VMAGEMIEFP 70 80 90 100 110 120 GGVYGLALNL KRDSVGAVIL GDSSTLAEGQ KGKCTGRILE VPVGKGLLGR VVDALGNPID 130 140 150 160 170 180 GKGPIESSGM SPIEKVAPGV VTRKSIDQPV QTGLKAIDAM IPVGRGQREL IIGDRQTGKT 190 200 210 220 230 240 AIAIDAIINQ KGTGVKCVYV AIGQKASSVA SIVRKLEEHG ALEHTIVVVA GASDSAALQY 250 260 270 280 290 300 IAPYAGCTMG EYFMERGEDA LIVYDDLTKQ AWAYRQISLL LRRPPGREAY PGDIFYLHSR 310 320 330 340 350 360 LLERAARINA DEVEKLTNGE VKGKTGSLTA LPIIETQAGD VSAFVPTNVI SITDGQIFLD 370 380 390 400 410 420 VDLFNSGVRP AINSGLSVSR VGGAAQTKIM KKLGGGTRLA LAQFRELEAF SQFASDLDDA 430 440 450 460 470 480 TRKQLERGQR ITELMKQKQY SPLTVAEMGV SLFVVEKGYL DDVPVNEISS FEASLHDYMR 490 500 510 STHAALLHAI NEAGAYDNEI EAKLKKAVEE FKNTGSW

References

[1]

"Identification and characterization of a new conjugation/ type IVA secretion system (trb/tra) of L. pneumophila Corby localized on a mobile genomic island." Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E., Steinert M., Buchrieser C., Hacker J., Heuner K. Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000675 Genomic DNA. Translation: ABQ57185.1.
RefSeq	YP_001252531.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A5III5.
Genome annotation databases
GeneID	5183074.
GenomeReviews	Gene locus LPC_3299 in contig CP000675_GR.
KEGG	lpc:LPC_3299.
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_LEGPC

Accession

Primary (citable) accession number: A5III5

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	June 26, 2007
Last modified:	November 3, 2009
This is version 26 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)