Reviewed, UniProtKB/Swiss-Prot Q5X0P1 (ATPA2_LEGPA)

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:	lpp3055

Organism

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

Taxonomic identifier

297246 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Legionellaceae › Legionella

Protein attributes

Sequence length	517 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 – 517	517	ATP synthase subunit alpha 2 HAMAP MF_01346		PRO_0000238271
Regions
	Nucleotide binding	173 – 180	8	ATP By similarity
Sites
	Site	377	1	Required for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5X0P1-1 [UniParc]. Last modified November 23, 2004. Version 1. Checksum: 406D720F0BC0A2F2	FASTA	517	55,528
	10 20 30 40 50 60 MSEQVALNPS EISELIRKKI DQFSVVSEAR NEGTIVSLKD GIVRLHGLAD VMAGEMIEFP 70 80 90 100 110 120 GGVYGLALNL ERDSVGAVIL GDSSTLAEGQ KGKCTGRILE VPVGKGLLGR VVDALGNPID 130 140 150 160 170 180 GKGPIESSGM SPIEKVAPGV ITRKSVDQPV QTGLKAIDAM IPVGRGQREL IIGDRQTGKT 190 200 210 220 230 240 AIAIDAIINQ KGTGVKCVYV AIGQKASSVA SIVRKLEEHG ALEHTIVVVA GASDSAALQY 250 260 270 280 290 300 IAPYSGCTMG 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]

"Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity." Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C. Nat. Genet. 36:1165-1173(2004) [PubMed: 15467720] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR628336 Genomic DNA. Translation: CAH14208.1.
RefSeq	YP_125357.1.
3D structure databases
SMR	Q5X0P1. Positions 33-512.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5X0P1.
Genome annotation databases
GeneID	3117604.
GenomeReviews	Gene locus lpp3055 in contig CR628336_GR.
KEGG	lpp:lpp3055.
Organism-specific databases
LegioList	lpp3055.
CMR	Search...
Phylogenomic databases
eggNOG	COG0056.
HOGENOM	HBG565875.
OMA	GSDRDIK.
Enzyme and pathway databases
BioCyc	LPNE297246:LPP3055-MONOMER.
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_LEGPA

Accession

Primary (citable) accession number: Q5X0P1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	November 23, 2004
Last modified:	February 9, 2010
This is version 46 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)