ID   L7WL26_TACUS            Unreviewed;       227 AA.
AC   L7WL26;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-NOV-2024, entry version 38.
DE   RecName: Full=ATP synthase subunit a {ECO:0000256|ARBA:ARBA00021312, ECO:0000256|RuleBase:RU004450};
GN   Name=ATP6 {ECO:0000313|EMBL:AGC81752.1};
GN   Synonyms=atp6 {ECO:0000313|EMBL:AFM53626.1};
OS   Tachysurus ussuriensis (Ussuri catfish) (Bagrus ussuriensis).
OG   Mitochondrion {ECO:0000313|EMBL:AGC81752.1}.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Bagridae; Tachysurus.
OX   NCBI_TaxID=1828414 {ECO:0000313|EMBL:AGC81752.1};
RN   [1] {ECO:0000313|EMBL:AFM53626.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=L1 {ECO:0000313|EMBL:AFM53626.1};
RA   Liu C.-C., Chen I.-S.;
RT   "Phylogeny of Amblycipiade and Bagridae catfish in Taiwan and Fujian,
RT   China.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AFV57274.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Liang H.W.;
RT   "The complete mitochondrial genome of Pseudobagrus ussuriensis.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AGC81752.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23351066; DOI=10.3109/19401736.2012.760079;
RA   Wan Q., Tao G., Cheng Q., Chen Y., Qiao H.;
RT   "The complete mitochondrial genome sequence of Pseudobagrus ussuriensis
RT   (Siluriformes: Bagridae).";
RL   Mitochondrial DNA 24:333-335(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. {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: Mitochondrion inner membrane
CC       {ECO:0000256|RuleBase:RU004450}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU004450}. Mitochondrion membrane
CC       {ECO:0000256|ARBA:ARBA00004225}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004225}.
CC   -!- SIMILARITY: Belongs to the ATPase A chain family.
CC       {ECO:0000256|ARBA:ARBA00006810}.
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DR   EMBL; JN116934; AFM53626.1; -; Genomic_DNA.
DR   EMBL; JX867258; AFV57274.1; -; Genomic_DNA.
DR   EMBL; KC188782; AGC81752.1; -; Genomic_DNA.
DR   AlphaFoldDB; L7WL26; -.
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:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:TreeGrafter.
DR   CDD; cd00310; ATP-synt_Fo_a_6; 1.
DR   FunFam; 1.20.120.220:FF:000004; ATP synthase subunit a; 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:0000256|ARBA:ARBA00023128, ECO:0000313|EMBL:AGC81752.1};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
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        69..89
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;  24869 MW;  B9775645A53310BE CRC64;
     MALNLFDQFM SPTHLGIPLI AIALTLPWIL VPAPTNRYQN NRLVSLQSWF IKTFTQQLLL
     PINQAGHKWA MILASLMIFI LTLNVLGLLP YTFTPTTQLS LNMGLAVPLW LATVIIGLRN
     QPTAALGHLL PEGTPVPLIP VLIIIETISL FIRPLALGVR LTANLTAGHL LIQLISTATI
     TLMPMMTTVA TLTAILLVLL TLLEVAVAVI QAYVFVLLLS LYLQENV
//