ID   ATP6_ALLMA              Reviewed;         262 AA.
AC   P50364;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=ATP synthase subunit a;
DE   AltName: Full=F-ATPase protein 6;
GN   Name=ATP6;
OS   Allomyces macrogynus.
OG   Mitochondrion.
OC   Eukaryota; Fungi; Fungi incertae sedis; Blastocladiomycota;
OC   Blastocladiomycota incertae sedis; Blastocladiomycetes; Blastocladiales;
OC   Blastocladiaceae; Allomyces.
OX   NCBI_TaxID=28583;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 46923 / Burma 3-35 (35OC);
RX   PubMed=7991539; DOI=10.1073/pnas.91.25.11807;
RA   Paquin B., Laforest M.-J., Lang B.F.;
RT   "Interspecific transfer of mitochondrial genes in fungi and creation of a
RT   homologous hybrid gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:11807-11810(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 46923 / Burma 3-35 (35OC);
RX   PubMed=8636971; DOI=10.1006/jmbi.1996.0056;
RA   Paquin B., Lang B.F.;
RT   "The mitochondrial DNA of Allomyces macrogynus: the complete genomic
RT   sequence from an ancestral fungus.";
RL   J. Mol. Biol. 255:688-701(1996).
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; U02039; AAA64932.1; -; Genomic_DNA.
DR   EMBL; U41288; AAC49231.1; -; Genomic_DNA.
DR   PIR; S63648; S63648.
DR   RefSeq; NP_043730.1; NC_001715.1.
DR   AlphaFoldDB; P50364; -.
DR   SMR; P50364; -.
DR   GeneID; 801875; -.
DR   VEuPathDB; FungiDB:AlmafMp11; -.
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   CHAIN           1..262
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_0000082082"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   262 AA;  28228 MW;  D086B3A57771B5FB CRC64;
     MFINLNPLEQ FSVYSATSAI LGSSSNSLAI TSLTNIAILF IIGLLVLTIF QISASSHLIK
     PTRWNIVLET WVASILGIVK DQIGNDAKNS LIYFPLIFTF FSFVFISNIL GMIPYSFTPT
     SHISVTLGLS IAIMIGVTLI GFSKHQLDFF SLFVPKGTPL ALVPLLVLIE FISYSARAFS
     LALRLTANVS AGHCLFGVIS ALSVSACIAV SSLLLKGITI TLPLAVLVVL YGLELLVALL
     QSYVFTLLTC SYLADVVNMG DH