Reviewed, UniProtKB/Swiss-Prot Q07YM0 (ATPA1_SHEFN)

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:	Sfri_3056

Organism

Shewanella frigidimarina (strain NCIMB 400) [Complete proteome] [HAMAP]

Taxonomic identifier

318167 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Shewanellaceae › Shewanella

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 1 HAMAP MF_01346		PRO_0000339057
Regions
	Nucleotide binding	176 – 183	8	ATP By similarity
Sites
	Site	369	1	Required for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q07YM0-1 [UniParc]. Last modified October 31, 2006. Version 1. Checksum: 6ABF3D63DC552315	FASTA	517	56,044
	10 20 30 40 50 60 MKLAPDLLQA TFEQTFSILQ QARRSFSPQL QPREIGTITS IATGIAKVSG LPGVGFEEIL 70 80 90 100 110 120 KFPSDIFGIA FNVDEDEIGA VLLGDYWHLQ AGDEVERCGH LVDVPVGEGL LGRIINPIGE 130 140 150 160 170 180 PLDGKGRLIA SARLPIERPS PAIMNRAPVS VPLQTGIKVI DALIPVGLGQ RELILGDRQT 190 200 210 220 230 240 GKTAIAVDTI LNQRDKNVLC VYCAIGQRAS GVAKVIATLH EQGALEYTVV VVTEGNDPPG 250 260 270 280 290 300 LAYIAPYAAT SIAEYFMQQG RNVLIVYDDL THHARAYREL SLLLRRPPGR EAFPGDIFYI 310 320 330 340 350 360 HSRLLERATH LSPNLGGGSL TALPIIETEA QDISAYIPTN LISITDGQIY LSPSLFELGV 370 380 390 400 410 420 LPAIDVGKSV SRVGGKAQRA AYRAVASNLK LAYAQFEELE TFASFGARLD DSTLKTIDHG 430 440 450 460 470 480 RRIRACLKQA ESTPISMIEQ IAVLLALTAN LFDEVPLDVM SQAEHAVRAA TADIPVEITA 490 500 510 RLASTEKLTD EDRDGILQPV RDALAPFMHS QKRKEIT

References

[1]

"Complete sequence of Shewanella frigidimarina NCIMB 400." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H., Newman D., Tiedje J.M. , Zhou J., Romine M.F., Culley D.E., Serres M., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000447 Genomic DNA. Translation: ABI72894.1.
RefSeq	YP_751733.1.
3D structure databases
SMR	Q07YM0. Positions 24-507.
ModBase	Search...
Protein-protein interaction databases
STRING	Q07YM0.
Genome annotation databases
GeneID	4279960.
GenomeReviews	Gene locus Sfri_3056 in contig CP000447_GR.
KEGG	sfr:Sfri_3056.
NMPDR	fig|318167.10.peg.2935.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0056.
HOGENOM	HBG565875.
OMA	NVLCVYC.
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

ATPA1_SHEFN

Accession

Primary (citable) accession number: Q07YM0

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	October 31, 2006
Last modified:	February 9, 2010
This is version 35 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)