ID F5HPX7_MERGA Unreviewed; 227 AA.
AC F5HPX7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 29-MAY-2024, entry version 32.
DE RecName: Full=ATP synthase subunit a {ECO:0000256|ARBA:ARBA00021312, ECO:0000256|RuleBase:RU004450};
GN Name=ATP6 {ECO:0000313|EMBL:BAK38523.1};
OS Merluccius gayi (South Pacific hake) (Merluccius gayi peruanus).
OG Mitochondrion {ECO:0000313|EMBL:BAK38523.1}.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Merlucciidae; Merluccius.
OX NCBI_TaxID=89948 {ECO:0000313|EMBL:BAK38523.1};
RN [1] {ECO:0000313|EMBL:BAK38523.1}
RP NUCLEOTIDE SEQUENCE.
RA Namikoshi A., Takashima Y., Iguchi J., Yanagimoto T., Yamashita M.;
RT "Species identification of Alaska pollock, Gadus spp., and Micromesistius
RT spp. in cod roe products using a PCR-based method.";
RL Fish. Sci. 77:671-678(2011).
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. {ECO:0000256|ARBA:ARBA00002070}.
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:0000256|ARBA:ARBA00011648}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC inner membrane {ECO:0000256|RuleBase:RU004450}; Multi-pass membrane
CC protein {ECO:0000256|RuleBase:RU004450}.
CC -!- SIMILARITY: Belongs to the ATPase A chain family.
CC {ECO:0000256|ARBA:ARBA00006810}.
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DR EMBL; AB571070; BAK38523.1; -; Genomic_DNA.
DR AlphaFoldDB; F5HPX7; -.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IEA:TreeGrafter.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:TreeGrafter.
DR CDD; cd00310; ATP-synt_Fo_a_6; 1.
DR Gene3D; 1.20.120.220; ATP synthase, F0 complex, subunit A; 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 NCBIfam; TIGR01131; ATP_synt_6_or_A; 1.
DR PANTHER; PTHR11410; ATP SYNTHASE SUBUNIT A; 1.
DR PANTHER; PTHR11410:SF0; ATP SYNTHASE SUBUNIT A; 1.
DR Pfam; PF00119; ATP-synt_A; 1.
DR PRINTS; PR00123; ATPASEA.
DR SUPFAM; SSF81336; F1F0 ATP synthase subunit A; 1.
DR PROSITE; PS00449; ATPASE_A; 1.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310};
KW CF(0) {ECO:0000256|ARBA:ARBA00022547};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Mitochondrion {ECO:0000313|EMBL:BAK38523.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 69..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 171..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 227 AA; 25107 MW; 7A9A6C8D89429664 CRC64;
MTLSLFDQFE SPTFMGIPLI MLALALPWLL FPAPTHRWLN SRVLALQGWF ISNFTSQIFS
PLNRGGHKWA LLLSALMIFL LTLNTLGLLP YTFTPTTQLA LNMALAVPLW LATVILGLRH
QITHALAHFL PEGTPTPLIP VLIIIETISL FIRPLALGVR LTANLTAGHL LIHLVSSAAF
VLLPLMPTVA FLTALLLFML TLLEIAVALI QAYVFVLLLS LYLQENV
//