Reviewed, UniProtKB/Swiss-Prot B0BZL2 (ATPA1_ACAM1)

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:	AM1_0896

Organism

Acaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]

Taxonomic identifier

329726 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Acaryochloris

Protein attributes

Sequence length	505 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 four main subunits: a1, b1, b'1 and c(9-12) By similarity. HAMAP MF_01346
Subcellular location	Cellular thylakoid 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) Membrane Thylakoid
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 proton-transporting ATP synthase complex, catalytic core F(1) Inferred from electronic annotation. Source: UniProtKB-KW thylakoid 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 – 505	505	ATP synthase subunit alpha 1 HAMAP MF_01346		PRO_0000339009
Regions
	Nucleotide binding	170 – 177	8	ATP By similarity
Sites
	Site	363	1	Required for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	B0BZL2-1 [UniParc]. Last modified February 26, 2008. Version 1. Checksum: F52CB721F5B1259D	FASTA	505	54,611
	10 20 30 40 50 60 MVSIRPDEIS NIIRQQIEQY DQQVKVDNVG TVLQVGDGIA RVYGLEQAMA GELLDFEDGT 70 80 90 100 110 120 VGIALNLEED NVGAVLMGDG RDLQEGSTVR STGKIAQIPV GDALIGRVLD ALARPIDGKG 130 140 150 160 170 180 DINTSETRLI ESPAPGIIER KSVYEPMQTG ITAIDSMVPI GRGQRELIIG DRQTGKTAVA 190 200 210 220 230 240 IDTILNQKSE DVICVYVAIG QKASTVAQVV EVLRERGALD YTVVVAANAN DPATLQYLAP 250 260 270 280 290 300 YTGAAIAEYF MYNGKHTLVI YDDLSKQAQA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE 310 320 330 340 350 360 RAAKLSPELG EGSMTALPIV ETQAGDVSAY IPTNVISITD GQIFLSSDLF NAGLRPAINA 370 380 390 400 410 420 GISVSRVGSA AQIKAMKQVA GKLKLELAQF AELEAFAQFA SDLDQATQNQ LARGARLREI 430 440 450 460 470 480 LKQPQYSPLP VEEMVAVIYA GTNGYLDDVP TDKVTEFVQG MRDDLKANHA KYGELVRSEK 490 500 KMGDEAEGIL KTAIADFKKS FMAAV

References

[1]

"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina." Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. , Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W. Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed: 18252824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000828 Genomic DNA. Translation: ABW25938.1.
RefSeq	YP_001515252.1.
3D structure databases
SMR	B0BZL2. Positions 25-501.
ModBase	Search...
Genome annotation databases
GeneID	5679722.
GenomeReviews	Gene locus AM1_0896 in contig CP000828_GR.
KEGG	amr:AM1_0896.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG565875.
OMA	GSDRDIK.
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

ATPA1_ACAM1

Accession

Primary (citable) accession number: B0BZL2

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	February 26, 2008
Last modified:	February 9, 2010
This is version 20 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)