Reviewed, UniProtKB/Swiss-Prot Q8Y4C0 (ATPA2_LISMO)

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:	lmo2531

Organism

Listeria monocytogenes [Complete proteome] [HAMAP]

Taxonomic identifier

1639 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Listeriaceae › Listeria

Protein attributes

Sequence length	504 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 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 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 – 504	504	ATP synthase subunit alpha 2 HAMAP MF_01346		PRO_0000238280
Regions
	Nucleotide binding	169 – 176	8	ATP By similarity
Sites
	Site	362	1	Required for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8Y4C0-1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 02EA58BE90D404A0	FASTA	504	55,087
	10 20 30 40 50 60 MSIKAEEISS IIKQQIENYH SELKVSDVGT VTYIGDGIAR AHGLDNAMAG ELLEFSNGVM 70 80 90 100 110 120 GMAQNLETND VGIIILGPYT EIREGDEVRR TGKIMEVPVG EALIGRVVNS LGQPVDGLGP 130 140 150 160 170 180 IETTGTRPIE AVAPGVMQRQ SVNEPLQTGI KAIDALVPIG RGQRELIIGD RQTGKTSVAI 190 200 210 220 230 240 DTILNQADQD MICIYVAIGQ KESTVRNAVE TLRHHGALDY TIVVTAAASQ PAPLLYLAPY 250 260 270 280 290 300 AGVAMAEEFM YNGKHVLVVY DDLSKQAAAY RELSLLLRRP PGREAYPGDV FYLHSRLLER 310 320 330 340 350 360 AAKLNDSLGG GSITALPFVE TQAGDISAYI PTNVISITDG QIFLQSDLFF SGVRPAINAG 370 380 390 400 410 420 LSVSRVGGSA QIKAMKTVAG TLRLDLAAYR ELESFSQFGS DLDAATRAKL ERGKRTVEVL 430 440 450 460 470 480 KQDLHKPLKV EKQVLILYAL VHKYLDDVPV HDVLRFESEM NTWFDHNHPE LLEEIRTTKK 490 500 LPDEAKLEAA LKEFKNTFVP SEEK

References

[1]

"Comparative genomics of Listeria species." Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. , Durant L., Dussurget O., Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P. Science 294:849-852(2001) [PubMed: 11679669] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-679 / EGD-e / Serovar 1/2a.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL591983 Genomic DNA. Translation: CAD00609.1.
PIR	AC1391.
RefSeq	NP_466054.1.
3D structure databases
SMR	Q8Y4C0. Positions 21-502.
ModBase	Search...
Genome annotation databases
GeneID	986486.
KEGG	lmo:lmo2531.
Organism-specific databases
ListiList	LMO2531.
CMR	Search...
Phylogenomic databases
HOGENOM	HBG565875.
OMA	EVVTELM.
Enzyme and pathway databases
BioCyc	LMON169963:LMO2531-MONOMER.
BRENDA	3.6.3.14. 96770.
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_LISMO

Accession

Primary (citable) accession number: Q8Y4C0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	March 1, 2002
Last modified:	February 9, 2010
This is version 54 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)