Q2RFX3 (ATP6_MOOTA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP synthase subunit a

Alternative name(s):
ATP synthase F0 sector subunit a
F-ATPase subunit 6

Gene names

Name:	atpB
Ordered Locus Names:	Moth_2384

Organism

Moorella thermoacetica (strain ATCC 39073) [Reference proteome] [HAMAP]

Taxonomic identifier

264732 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacteraceae › Moorella group › Moorella › Moorella thermoacetica

Protein attributes

Sequence length	218 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane By similarity. HAMAP-Rule MF_01393
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. In this bacterium the a and b subunits are transcribed but do not seem to be translated, thus the ATP synthase consists of the alpha, beta, gamma, delta, epsilon and c subunits. Ref.1
Subcellular location	Cell membrane; Multi-pass membrane protein Probable HAMAP-Rule MF_01393.
Sequence similarities	Belongs to the ATPase A chain family.
Sequence caution	The sequence AAB51460.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(0) Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	plasma membrane ATP synthesis coupled proton transport Inferred from electronic annotation. Source: HAMAP
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell proton-transporting ATP synthase complex, coupling factor F(o) Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	proton-transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 218	218	ATP synthase subunit a HAMAP-Rule MF_01393		PRO_0000362350
Regions
	Transmembrane	17 – 37	21	Helical; Potential
	Transmembrane	75 – 95	21	Helical; Potential
	Transmembrane	104 – 124	21	Helical; Potential
	Transmembrane	162 – 184	23	Helical; Potential
	Transmembrane	196 – 216	21	Helical; Potential

Sequences

	Sequence		Length	Mass (Da)
	Q2RFX3 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: E83F4F294FA575F5	FASTA	218	24,723
	10 20 30 40 50 60 MTHVRPVEIF HLGPIPIYST VVNTWIIMIL LLAGIFLATR KLSFIPRGAQ HVLEMFLEFF 70 80 90 100 110 120 YGLLEEIIGK EGRRYLPLVA TLFIFILSLN LSWFIPGMKP PTMDLSTTAA FAVTTIILVQ 130 140 150 160 170 180 IFGIRKLGLR GYIRHFFQPA PFLFPLNVIE ELVKPVSLSL RLFGNLFGEE MVVTILFLMI 190 200 210 PFLLPTPIML LGVLMGTIQA FVFTLLTITY IANFVHGH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Composition and primary structure of the F1F0 ATP synthase from the obligately anaerobic bacterium Clostridium thermoaceticum." Das A., Ljungdahl L.G. J. Bacteriol. 179:3746-3755(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, TRANSCRIPT, OPERON STRUCTURE.
[2]	"The complete genome sequence of Moorella thermoacetica (f. Clostridium thermoaceticum)." Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C., Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W. Environ. Microbiol. 10:2550-2573(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39073.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U64318 Genomic DNA. Translation: AAB51460.1. Different initiation. CP000232 Genomic DNA. Translation: ABC20666.1.
RefSeq	YP_431209.1. NC_007644.1.
3D structure databases
ProteinModelPortal	Q2RFX3.
ModBase	Search...
Protein-protein interaction databases
STRING	264732.Moth_2384.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABC20666; ABC20666; Moth_2384.
GeneID	3832023.
KEGG	mta:Moth_2384.
PATRIC	22642266. VBIMooThe6753_2597.
Phylogenomic databases
eggNOG	COG0356.
HOGENOM	HOG000253873.
KO	K02108.
OMA	QVFLTSW.
Enzyme and pathway databases
BioCyc	MTHE264732:GH0A-2474-MONOMER.
Family and domain databases
Gene3D	1.20.120.220. 1 hit.
HAMAP	MF_01393. ATP_synth_a_bact.
InterPro	IPR000568. ATPase_F0-cplx_asu. IPR023011. ATPase_F0-cplx_asu_AS. [Graphical view]
PANTHER	PTHR11410. PTHR11410. 1 hit.
Pfam	PF00119. ATP-synt_A. 1 hit. [Graphical view]
PRINTS	PR00123. ATPASEA.
SUPFAM	SSF81336. ATPase_F0_A. 1 hit.
TIGRFAMs	TIGR01131. ATP_synt_6_or_A. 1 hit.
PROSITE	PS00449. ATPASE_A. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATP6_MOOTA

Accession

Primary (citable) accession number: Q2RFX3
Secondary accession number(s): O05428

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	January 24, 2006
Last modified:	May 1, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program