O51121 (VATA_BORBU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
V-type ATP synthase alpha chain
EC=3.6.3.14

Alternative name(s):
V-ATPase subunit A

Gene names

Name:	atpA
Ordered Locus Names:	BB_0094

Organism

Borrelia burgdorferi (Lyme disease spirochete)

Taxonomic identifier

139 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group

Protein attributes

Sequence length	575 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 V-type alpha chain is a catalytic subunit. HAMAP MF_00309
Catalytic activity	ATP + H2O + H+(In) = ADP + phosphate + H+(Out). HAMAP MF_00309
Sequence similarities	Belongs to the ATPase alpha/beta chains family.
Sequence caution	The sequence AAC66483.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro
Cellular component	proton-transporting two-sector ATPase complex, catalytic domain Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW hydrogen ion transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro 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 – 575	575	V-type ATP synthase alpha chain HAMAP MF_00309		PRO_0000144609
Regions
	Nucleotide binding	238 – 245	8	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	O51121 [UniParc]. Last modified January 24, 2001. Version 2. Checksum: 232B62C1904FE26F	FASTA	575	64,033
	10 20 30 40 50 60 MNTKGKVVGV NGNLVTIEVE GSVSMNEVLF VKTAGRNLKA EVIRIRGNEV DAQVFELTKG 70 80 90 100 110 120 ISVGDLVEFT DKLLTVELGP GLLTQVYDGL QNPLPELAIQ CGFFLERGVY LRPLNKDKKW 130 140 150 160 170 180 NFKKTSKVGD IVIAGDFLGF VIEGTVHHQI MIPFYKRDSY KIVEIVSDGD YSIDEQIAVI 190 200 210 220 230 240 EDDSGMRHNI TMSFHWPVKV PITNYKERLI PSEPMLTQTR IIDTFFPVAK GGTFCIPGPF 250 260 270 280 290 300 GAGKTVLQQV TSRNADVDVV IIAACGERAG EVVETLKEFP ELMDPKTGKS LMDRTCIICN 310 320 330 340 350 360 TSSMPVAARE ASVYTAITIG EYYRQMGLDI LLLADSTSRW AQAMREMSGR LEEIPGEEAF 370 380 390 400 410 420 PAYLESVIAS FYERAGIVVL NNGDIGSVTV GGSVSPAGGN FEEPVTQATL KVVGAFHGLT 430 440 450 460 470 480 RERSDARKFP AISPLESWSK YKGVIDQKKT EYARSFLVKG NEINQMMKVV GEEGISNDDF 490 500 510 520 530 540 LIYLKSELLD SCYLQQNSFD SIDAAVSSER QNYMFDIVYN ILKTNFEFSD KLQARDFINE 550 560 570 LRQNLLDMNL SSFKDHKFNK LEHALGELIN FKKVI

References

[1]

"Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi." Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J. , Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B., Smith H.O., Venter J.C. Nature 390:580-586(1997) [PubMed: 9403685] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000783 Genomic DNA. Translation: AAC66483.1. Different initiation.
PIR	F70111.
RefSeq	NP_212228.2. NC_001318.1.
3D structure databases
ProteinModelPortal	O51121.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBORT00000008365; EBBORP00000007695; EBBORG00000008364.
GeneID	1194930.
GenomeReviews	Gene locus BB_0094 in contig AE000783_GR.
KEGG	bbu:BB0094.
NMPDR	fig|224326.1.peg.478.
PATRIC	20556794. VBIBorBur75917_0492.
TIGR	BB_0094.
Phylogenomic databases
GeneTree	EBGT00050000006810.
HOGENOM	HBG288114.
OMA	SRWAQAM.
ProtClustDB	PRK04192.
Enzyme and pathway databases
BioCyc	BBUR224326:BB_0094-MONOMER.
Family and domain databases
HAMAP	MF_00309. ATP_synth_A_arch. [Tree]
InterPro	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. IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd. IPR022878. V-ATPase_su_A/alpha. [Graphical view]
KO	K02117.
Pfam	PF00006. ATP-synt_ab. 1 hit. PF00306. ATP-synt_ab_C. 1 hit. PF02874. ATP-synt_ab_N. 1 hit. [Graphical view]
SUPFAM	SSF50615. ATPase_a/b_N. 1 hit.
PROSITE	PS00152. ATPASE_ALPHA_BETA. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

VATA_BORBU

Accession

Primary (citable) accession number: O51121

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	January 24, 2001
Last modified:	January 25, 2012
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program