ATP6_ASHGO
ID ATP6_ASHGO Reviewed; 263 AA.
AC Q75G39;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=ATP synthase subunit a;
DE AltName: Full=F-ATPase protein 6;
DE Flags: Precursor;
GN Name=ATP6; OrderedLocusNames=AMI006W; ORFNames=AgATP6;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC Complex V) produces ATP from ADP in the presence of a proton gradient
CC across the membrane which is generated by electron transport complexes
CC of the respiratory chain. F-type ATPases consist of two structural
CC domains, F(1) - containing the extramembraneous catalytic core and F(0)
CC - containing the membrane proton channel, linked together by a central
CC stalk and a peripheral stalk. During catalysis, ATP synthesis in the
CC catalytic domain of F(1) is coupled via a rotary mechanism of the
CC central stalk subunits to proton translocation. Key component of the
CC proton channel; it may play a direct role in the translocation of
CC protons across the membrane.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. In yeast, the dimeric form
CC of ATP synthase consists of 18 polypeptides: alpha, beta, gamma, delta,
CC epsilon, 4 (B), 5 (OSCP), 6 (A), 8, 9 (C), d, E (Tim11), f, g, h, i, j
CC and k.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE016821; AAS50173.1; -; Genomic_DNA.
DR RefSeq; NP_987083.1; NC_005789.1.
DR AlphaFoldDB; Q75G39; -.
DR SMR; Q75G39; -.
DR STRING; 33169.AAS50173; -.
DR EnsemblFungi; AAS50173; AAS50173; AGOS_AMI006W.
DR GeneID; 2760773; -.
DR KEGG; ago:AGOS_AMI006W; -.
DR eggNOG; KOG4665; Eukaryota.
DR HOGENOM; CLU_041018_0_2_1; -.
DR InParanoid; Q75G39; -.
DR OMA; FFDQFMS; -.
DR Proteomes; UP000000591; Mitochondrion.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:EnsemblFungi.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:EnsemblFungi.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR Gene3D; 1.20.120.220; -; 1.
DR HAMAP; MF_01393; ATP_synth_a_bact; 1.
DR InterPro; IPR000568; ATP_synth_F0_asu.
DR InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR InterPro; IPR045083; ATP_synth_F0_asu_bact/mt.
DR InterPro; IPR035908; F0_ATP_A_sf.
DR PANTHER; PTHR11410; PTHR11410; 1.
DR Pfam; PF00119; ATP-synt_A; 1.
DR PRINTS; PR00123; ATPASEA.
DR SUPFAM; SSF81336; SSF81336; 1.
DR TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1.
DR PROSITE; PS00449; ATPASE_A; 1.
PE 3: Inferred from homology;
KW ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT PROPEP 1..14
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000002606"
FT CHAIN 15..263
FT /note="ATP synthase subunit a"
FT /id="PRO_0000002607"
FT TRANSMEM 35..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..250
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 263 AA; 30052 MW; C5CB277DA2896239 CRC64;
MYLNNNNNMK YYINSPLEQF EIRDLLGLTS PMMDFSFINI TNFGLYTMIT LLVILTMNLM
TNNYNKLVGS NWYLSQEMIY DTIMNMVKTQ IGGKVWGYYF PLVYTFFITI FTMNLISMIP
YSFAMTSHVV FVVSMSMIIW LGTTIIGFYT HGLKFFGLFL PTGTPLILVP LLVSIELLSY
FARTISLGLR LSANIMAGHL LIVILGGLLF NLMAMNILTF LLGFLPMIAI LGIVCLEFAI
TIIQAYVWCI LMSSYLKDTI YLH
