ID   ATP6_STRCA              Reviewed;         227 AA.
AC   O21402;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=ATP synthase subunit a;
DE   AltName: Full=F-ATPase protein 6;
GN   Name=MT-ATP6; Synonyms=ATP6, ATPASE6, MTATP6;
OS   Struthio camelus (Common ostrich).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC   Struthio.
OX   NCBI_TaxID=8801;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9214748; DOI=10.1093/oxfordjournals.molbev.a025815;
RA   Harlid A., Janke A., Arnason U.;
RT   "The mtDNA sequence of the ostrich and the divergence between paleognathous
RT   and neognathous birds.";
RL   Mol. Biol. Evol. 14:754-761(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Sorenson M.D., Dimcheff D.E., Ast J.C., Yuri T., Mindell D.P.;
RT   "Primers for a PCR-based approach to complete mitochondrial genome
RT   sequencing.";
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11370967; DOI=10.1098/rspb.2001.1587;
RA   Haddrath O., Baker A.J.;
RT   "Complete mitochondrial DNA genome sequences of extinct birds: ratite
RT   phylogenetics and the vicariance biogeography hypothesis.";
RL   Proc. R. Soc. B 268:939-945(2001).
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.
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; Y12025; CAA72749.1; -; Genomic_DNA.
DR   EMBL; AF069429; AAD09388.1; -; Genomic_DNA.
DR   EMBL; AF338715; AAK53345.1; -; Genomic_DNA.
DR   PIR; F90612; F90612.
DR   PIR; T12414; T12414.
DR   RefSeq; NP_115446.1; NC_002785.1.
DR   AlphaFoldDB; O21402; -.
DR   SMR; O21402; -.
DR   GeneID; 803276; -.
DR   CTD; 4508; -.
DR   OrthoDB; 1095315at2759; -.
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_0000082173"
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        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        196..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   227 AA;  25048 MW;  338E70B269303347 CRC64;
     MNLSFFDQFA SPQLLGIPLI LLSLLFPTLL LPSPNNRWIN NRLSTLQLWF LQLITKQLMM
     PLNKAGHKWA LILTSLMTFL LLINLLGLLP YTFTPTTQLS MNMALAFPLW LATLLTGLRN
     QPSISLGHLL PEGTPTPLIP ALILIETTSL LIRPLALGVR LTANLTAGHL LIQLISTATL
     ALLPTMPTIS VLTATVLLLL TILELAVAMI QAYVFVLLLS LYLQENI