ATP6_DROSE
ID ATP6_DROSE Reviewed; 224 AA.
AC Q7IV45;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=ATP synthase subunit a;
DE AltName: Full=F-ATPase protein 6;
GN Name=mt:ATPase6; Synonyms=ATP6, ATPase6;
OS Drosophila sechellia (Fruit fly).
OG Mitochondrion {ECO:0000312|EMBL:AAF77281.1}.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25 {ECO:0000312|Proteomes:UP000001292};
RX PubMed=10903372; DOI=10.1007/s002390010066;
RA Ballard J.W.O.;
RT "Comparative genomics of mitochondrial DNA in members of the Drosophila
RT melanogaster subgroup.";
RL J. Mol. Evol. 51:48-63(2000).
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. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000255}.
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DR EMBL; AF200832; AAF77281.1; -; Genomic_DNA.
DR RefSeq; NP_982313.1; NC_005780.1.
DR AlphaFoldDB; Q7IV45; -.
DR SMR; Q7IV45; -.
DR STRING; 7238.Q7IV45; -.
DR GeneID; 2760941; -.
DR KEGG; dse:2760941; -.
DR CTD; 4508; -.
DR FlyBase; FBgn0041969; Dsec\mt:ATPase6.
DR Proteomes; UP000001292; Mitochondrion.
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; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..224
FT /note="ATP synthase subunit a"
FT /id="PRO_0000233912"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 224 AA; 25069 MW; D91683DE45AD44A5 CRC64;
MMTNLFSVFD PSAIFNLSLN WLSTFLGILM IPSIYWLMPS RYNIVWNSIL LTLHKEFKTL
LGPSGHNGST FIFISLFSLI LFNNFMGLFP YIFTSTSHLT LTLSLALPLW LCFMMYGWIN
HTQHMFAHLV PQGTPAVLMP FMVCIETISN IIRPGTLAVR LTANMIAGHL LLTLLGNTGP
SMSYLLVTFL LTAQIALLVL ESAVAMIQSY VFAVLSTLYS SEVN
