ID   ATP6_BRALA              Reviewed;         227 AA.
AC   O21004; O79419;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=ATP synthase subunit a;
DE   AltName: Full=F-ATPase protein 6;
GN   Name=ATP6;
OS   Branchiostoma lanceolatum (Common lancelet) (Amphioxus lanceolatum).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomidae; Branchiostoma.
OX   NCBI_TaxID=7740;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9332712; DOI=10.1023/a:1021954109452;
RA   Delarbre C., Gachelin G.;
RT   "A unique cDNA coding for subunits 8 and 6 of mitochondrial adenosine
RT   triphosphatase of the lancelet Branchiostoma lanceolatum, an ancestor of
RT   vertebrates.";
RL   Biochem. Genet. 35:181-187(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9628930; DOI=10.1093/nar/26.13.3279;
RA   Spruyt N., Delarbre C., Gachelin G., Laudet V.;
RT   "Complete sequence of the amphioxus (Branchiostoma lanceolatum)
RT   mitochondrial genome: relations to vertebrates.";
RL   Nucleic Acids Res. 26:3279-3285(1998).
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. CF(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC       subunits: a, b and c (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000305}.
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DR   EMBL; Y09525; CAA70712.1; -; Genomic_DNA.
DR   EMBL; Y16474; CAA76252.1; -; Genomic_DNA.
DR   PIR; G71390; G71390.
DR   RefSeq; NP_007542.1; NC_001912.1.
DR   AlphaFoldDB; O21004; -.
DR   SMR; O21004; -.
DR   GeneID; 808214; -.
DR   CTD; 4508; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR   GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
DR   Gene3D; 1.20.120.220; -; 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; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..227
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_0000082096"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        205..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        49
FT                   /note="V -> A (in Ref. 1; CAA70712)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        111..113
FT                   /note="FGT -> LGS (in Ref. 1; CAA70712)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   227 AA;  25136 MW;  41EA1D3532AA7023 CRC64;
     MMVSLFSQFD SPWLLNIPLV LLALIMPWKL FVSFGPSWAG TRSSRLVYVT METLMSQVMQ
     PLNKLGFRWV VLFSSLMLML MTLNVIGLFP YTFTPTTQLS MNLGLAVPLW FGTVVYGFRN
     HPVIALAHLC PEGAPNLLVP VLVVVETLSI LMRPLALGLR LTANLTAGHL LMHLISSAVL
     GLMELSVMLS GITLLLLVFL TMLEIAVALI QGYVFAILVT LYLDENL