Reviewed, UniProtKB/Swiss-Prot Q39ZT9 (ATPA1_PELCD)

Names and origin

Protein names

Recommended name:
    ATP synthase subunit alpha 1
    EC=3.6.3.14
Alternative name(s):
    F-ATPase subunit alpha 1
    ATP synthase F1 sector subunit alpha 1

Gene names

Name:	atpA1
Ordered Locus Names:	Pcar_0947, Pcar_3133

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	502 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 – 502	502	ATP synthase subunit alpha 1 HAMAP MF_01346		PRO_0000238313
Regions
	Nucleotide binding	169 – 176	8	ATP By similarity
Sites
	Site	362	1	Required for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q39ZT9-1 [UniParc]. Last modified November 22, 2005. Version 1. Checksum: 2F7F0A9479E9E8D5	FASTA	502	54,450
	10 20 30 40 50 60 MDIKAEEICA IIEQQIENFD REIEISEMGT IISVGDGIAR IHGLNRAMAG ELLEFPGDVI 70 80 90 100 110 120 GMVLNLEEDN VGAAILGDTH HIKEGDSVRR TGRIVEVPVG EALIGRVVNG IGQPIDGGGA 130 140 150 160 170 180 LEGAEARQVE IKAPGIVTRK SVHQPVQTGL KAIDALVPIG RGQRELIIGD RQTGKTALAI 190 200 210 220 230 240 DAIINQKGQD MVCIYVAIGQ KQSTVAQVVD KLKQHGAMDY TIVVSAGASE PAPLQFIAPY 250 260 270 280 290 300 AGVTMGEYFR DNGRHALIVY DDLSKHAVAY RQLSLLLRRP PGREAFPGDV FYLHSRLLER 310 320 330 340 350 360 AAKLNDELGG GSLTALPIIE TQAGDLSSYI PTNVISITDG QIFLEADLFY SGVRPAINVG 370 380 390 400 410 420 LSVSRVGGSA QVKAMKQVAG TLRLSLAQYR EMAAFAQFGS DLDAATQKQL ARGARLVEIL 430 440 450 460 470 480 KQPQYQPLPV EKQILVIYAA NNGYVDDYPL TVLRRYEEEL YSFLEHRHGD LLKDLAEKKA 490 500 IDTDLEARIK AVLAAFGEQF TP

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
EMBLGenBankDDBJ	CP000142 Genomic DNA. Translation: ABA90368.1. CP000142 Genomic DNA. Translation: ABA88200.1.
RefSeq	YP_356370.1. YP_358538.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q39ZT9.
Genome annotation databases
GeneID	3724127. 3725841.
GenomeReviews	Gene locus Pcar_0947 in contig CP000142_GR. Gene locus Pcar_3133 in contig CP000142_GR.
KEGG	pca:Pcar_0947. pca:Pcar_3133.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q39ZT9.
OMA	KQVAIIF.
Enzyme and pathway databases
BioCyc	PCAR338963:PCAR_0947-MON. PCAR338963:PCAR_3133-MON.
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. IPR020003. ATPase_F1/V1/A1_a/bsu_AS. IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd. IPR018538. HAS-barrel. [Graphical view]
PANTHER	PTHR15184:SF3. ATPase_F1_a. 1 hit.
Pfam	PF00006. ATP-synt_ab. 1 hit. PF00306. ATP-synt_ab_C. 1 hit. PF09378. HAS-barrel. 1 hit. [Graphical view]
TIGRFAMs	TIGR00962. atpA. 1 hit.
PROSITE	PS00152. ATPASE_ALPHA_BETA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATPA1_PELCD

Accession

Primary (citable) accession number: Q39ZT9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	November 22, 2005
Last modified:	November 3, 2009
This is version 36 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)