Reviewed, UniProtKB/Swiss-Prot Q3B3Z9 (ATPA1_PELLD)

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:	Plut_1070

Organism

Pelodictyon luteolum (strain DSM 273) (Chlorobium luteolum (strain DSM 273)) [Complete proteome] [HAMAP]

Taxonomic identifier

319225 [NCBI]

Taxonomic lineage

Bacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobium/Pelodictyon group › Pelodictyon

Protein attributes

Sequence length	511 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 four main subunits: a1, b1, b'1 and c(9-12) 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 – 511	511	ATP synthase subunit alpha 1 HAMAP MF_01346		PRO_0000238315
Regions
	Nucleotide binding	174 – 181	8	ATP By similarity
Sites
	Site	367	1	Required for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3B3Z9-1 [UniParc]. Last modified November 22, 2005. Version 1. Checksum: BD31C72CEAD22DC8	FASTA	511	55,555
	10 20 30 40 50 60 MQEKTLTESI DAALSSIGEA SRTTQPEIEL RENGVVTTVL NGIALIRGLP GVGYEELVEM 70 80 90 100 110 120 SGGVYGIAFN VDPDEVGVVL LGEYAKLQAG GRARRTGRVM DVPVGDGLLG RVVNPLGRPL 130 140 150 160 170 180 DAEGEPRFSG RLPIERPSPG IMDRNAVSTP LQTGLKVVDA IVPIGRGQRE LILGDRQTGK 190 200 210 220 230 240 TAIAVATILN QKGRNVICIY CAIGQRASAV AKVLAQLREH GAMAHTVAVV TEGNDPSGLQ 250 260 270 280 290 300 YIAPYAATSI GEYFMEQGRD VLIVYDDLTN HARAYRELSL LLKRPPGREA FPGDIFYVHS 310 320 330 340 350 360 RLLERSTHLR KELGGGSLTA LPIIETEAQN ISAYIPTNLI SITDGQIYLS PTLFELGNLP 370 380 390 400 410 420 AVDIGKSVSR VGGKAQLAAY RSVTGRLKLA YAQFEELENF ARFGTRLDEA SRKAITHGER 430 440 450 460 470 480 IRECLKQDEL DVLGVEEQIL ILLSLSEGQF DPLELSEVSG AMKRLSAAAR ELPRDLLERL 490 500 510 HSDRPLSDED RRRLLQTAEA ALQKKRTAGR L

References

[1]

"Complete sequence of Pelodictyon luteolum DSM 273." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P. Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000096 Genomic DNA. Translation: ABB23932.1.
RefSeq	YP_374975.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q3B3Z9.
Genome annotation databases
GeneID	3746254.
GenomeReviews	Gene locus Plut_1070 in contig CP000096_GR.
KEGG	plt:Plut_1070.
NMPDR	fig|319225.3.peg.786.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q3B3Z9.
OMA	NVLCVYC.
Enzyme and pathway databases
BioCyc	PLUT319225:PLUT_1070-MON.
Family and domain databases
HAMAP	MF_01346. [Tree]
InterPro	IPR017710. Alt_ATPase_F1-cplx_asu. IPR005294. ATPase_F1-cplx_asu. IPR017458. ATPase_F1-cplx_asu_C. 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_PELLD

Accession

Primary (citable) accession number: Q3B3Z9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	November 22, 2005
Last modified:	November 3, 2009
This is version 34 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)