Reviewed, UniProtKB/Swiss-Prot Q3A076 (ATPA2_PELCD)

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:	Pcar_2996

Organism

Pelobacter carbinolicus (strain DSM 2380 / Gra Bd 1) [Complete proteome] [HAMAP]

Taxonomic identifier

338963 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Deltaproteobacteria › Desulfuromonadales › Pelobacteraceae › Pelobacter

Protein attributes

Sequence length	522 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 – 522	522	ATP synthase subunit alpha 2 HAMAP MF_01346		PRO_0000238314
Regions
	Nucleotide binding	176 – 183	8	ATP By similarity
Sites
	Site	369	1	Required for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3A076-1 [UniParc]. Last modified November 22, 2005. Version 1. Checksum: 9C124C18F6EA589F	FASTA	522	56,469
	10 20 30 40 50 60 MKDTLPSATQ VLKEAFDTLD SALENFSPVL AVQHVGWVEY IGKGIARVGG LPGVRCEELL 70 80 90 100 110 120 AFPGGLLGLA LDADEDQVGV VLFGDYTHLQ AGDEVRRTGR VLDVPVGDGL IGRVVNPVGR 130 140 150 160 170 180 CLDGGKPVAF QRQLPVERPA PPIMDRLPVT QPLMTGIKVI DALIPIGRGQ RELILGDRQT 190 200 210 220 230 240 GKTAIAIDAI INQRDQDVVC IYCAIGQRAA SVAGVVTELR NCGALDYTIV VVAEGDAPPG 250 260 270 280 290 300 LQYIAPYAAT SMAEHFMEHG RDVLIVYDDL TRHARAYREI SLLLRRPPGR EAFPGDIFYV 310 320 330 340 350 360 HSRLLERATH LNEPRGGGSL TALPIIETEA QNLSAYIPTN LISITDGQIY LSPELFQKGL 370 380 390 400 410 420 LPSVDVGKSV SRVGGKTQLA AYRAVAGDLR LTYAQFEELE AFARFGTRLD EETRQVLHRG 430 440 450 460 470 480 RRVRAILKQT QSSPRTAPQQ VLVLHSLNSG VFDTVDEEAL PAAEQAICAA VSEIPEIVDK 490 500 510 520 ILQGKTLSQE DLDVMHTVAK RVTRPFIKLG EEGHAGAAGD AT

References

[1]

"Complete sequence of Pelobacter carbinolicus DSM 2380." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P. Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000142 Genomic DNA. Translation: ABA90231.1.
RefSeq	YP_358401.1.
3D structure databases
SMR	Q3A076. Positions 24-506.
ModBase	Search...
Protein-protein interaction databases
STRING	Q3A076.
Genome annotation databases
GeneID	3725703.
GenomeReviews	Gene locus Pcar_2996 in contig CP000142_GR.
KEGG	pca:Pcar_2996.
NMPDR	fig|338963.3.peg.2969.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0056.
HOGENOM	HBG565875.
OMA	NVLCVYC.
Enzyme and pathway databases
BioCyc	PCAR338963:PCAR_2996-MONOMER.
Family and domain databases
HAMAP	MF_01346. ATP_synth_alpha_bact. [Tree]
InterPro	IPR017710. Alt_ATPase_F1-cplx_asu. 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	TIGR03324. alt_F1F0_F1_al. 1 hit. TIGR00962. atpA. 1 hit.
PROSITE	PS00152. ATPASE_ALPHA_BETA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATPA2_PELCD

Accession

Primary (citable) accession number: Q3A076

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	November 22, 2005
Last modified:	February 9, 2010
This is version 39 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)