ID   ATP6_TRYBB              Reviewed;         229 AA.
AC   P24499;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=ATP synthase subunit a;
DE   AltName: Full=F-ATPase protein 6;
GN   Name=ATP6; Synonyms=MURF4;
OS   Trypanosoma brucei brucei.
OG   Mitochondrion.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=5702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2140530; DOI=10.1016/0092-8674(90)90199-o;
RA   Bhat G.J., Koslowsky D.J., Feagin J.E., Smiley B.L., Stuart K.;
RT   "An extensively edited mitochondrial transcript in kinetoplastids encodes a
RT   protein homologous to ATPase subunit 6.";
RL   Cell 61:885-894(1990).
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; M33228; AAA97428.1; ALT_SEQ; mRNA.
DR   AlphaFoldDB; P24499; -.
DR   SMR; P24499; -.
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:0006754; P:ATP biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..229
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_0000082181"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        143..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        177..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        206..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   229 AA;  28330 MW;  6EA6F1051C60AA4C CRC64;
     MFLFFFCDLF WLRLLLCMYY CVSRLCFIVY FNCLMLIFDF LLFCLFDLYL FVGLCLFLLL
     WFMLFNLYSL ILYYCITYLN LYLLFCIVFL LYIAFLFLFC FLCDFFLFNN LLVGDSFMDV
     FFIRFLLCFL ECFSLLCRCL STFLRLFCNL LSSHFLLLMF FDFFYFIFVF FFYGVFCYFI
     LFIFVFCFCL LFYVFLYLLD LFAAILQLFI FCNMILQLIM DFLLFLLFV