ID   ATP6_ZANCU              Reviewed;         248 AA.
AC   Q3T4C2;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=ATP synthase subunit a {ECO:0000250|UniProtKB:Q03671};
DE   AltName: Full=ATP synthase subunit 6 {ECO:0000250|UniProtKB:Q03671};
DE   AltName: Full=F-ATPase protein 6 {ECO:0000250|UniProtKB:Q03671};
DE   Flags: Precursor;
GN   Name=atp6 {ECO:0000312|EMBL:AAW49492.1};
OS   Zancudomyces culisetae (Gut fungus) (Smittium culisetae).
OG   Mitochondrion {ECO:0000312|EMBL:AAW49492.1}.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC   Harpellomycetes; Harpellales; Legeriomycetaceae; Zancudomyces.
OX   NCBI_TaxID=1213189;
RN   [1] {ECO:0000312|EMBL:AAW49492.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=18-3 {ECO:0000312|EMBL:AAW49492.1};
RX   PubMed=15689432; DOI=10.1093/nar/gki199;
RA   Seif E., Leigh J., Liu Y., Roewer I., Forget L., Lang B.F.;
RT   "Comparative mitochondrial genomics in zygomycetes: bacteria-like RNase P
RT   RNAs, mobile elements, and a close source of the group I intron invasion in
RT   angiosperms.";
RL   Nucleic Acids Res. 33:734-744(2005).
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:0000305}.
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 {ECO:0000305};
CC       Multi-pass membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000255}.
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DR   EMBL; AY863213; AAW49492.1; -; Genomic_DNA.
DR   RefSeq; YP_203325.1; NC_006837.1.
DR   AlphaFoldDB; Q3T4C2; -.
DR   SMR; Q3T4C2; -.
DR   GeneID; 3260114; -.
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   HAMAP; MF_01393; ATP_synth_a_bact; 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   PROPEP          1..3
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:Q03671"
FT                   /id="PRO_0000391440"
FT   CHAIN           4..248
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_0000391441"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        183..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        227..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   248 AA;  27680 MW;  1DC75A02050C2233 CRC64;
     MLYNPLEQFT VNKIISLYTV YYSMSLTNSS LYFIIAAIIS FFIFKYSANI PYVSLINKNN
     YSILTESLYK TILKMVKEQI GDKYTIYMPL IFSLFIIILV SNLVGLIPYG FSPTALFALP
     LGLSVTIIIS VTVIGFVKYH LKYFSVLLPS GTPLGLVPLL LVVELLSYIA RAFSLGIRLA
     ANITSGHILL NIISGFLFKT SGIALLFVII PFTLFIALTG LELIVAILQA YVWSILTCIY
     IKDSLILH