ATP6_ALLAR
ID ATP6_ALLAR Reviewed; 262 AA.
AC P50363; Q7IKZ8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=ATP synthase subunit a;
DE AltName: Full=F-ATPase protein 6;
GN Name=ATP6;
OS Allomyces arbusculus (Aquatic fungus).
OG Mitochondrion.
OC Eukaryota; Fungi; Fungi incertae sedis; Blastocladiomycota;
OC Blastocladiomycota incertae sedis; Blastocladiomycetes; Blastocladiales;
OC Blastocladiaceae; Allomyces.
OX NCBI_TaxID=64504;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10983;
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].
RX PubMed=11070063; DOI=10.1093/oxfordjournals.molbev.a026274;
RA Paquin B., Laforest M.-J., Lang B.F.;
RT "Double-hairpin elements in the mitochondria DNA of Allomyces: Evidence for
RT mobility.";
RL Mol. Biol. Evol. 17:1760-1768(2000).
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; U02038; AAA64931.1; -; Genomic_DNA.
DR EMBL; AF281324; AAF99320.1; -; Genomic_DNA.
DR AlphaFoldDB; P50363; -.
DR SMR; P50363; -.
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_0000082081"
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; 28276 MW; 8BD9CD8DC5CDAC70 CRC64;
MFINLNPLEQ FSVYSATSAI LGSSSNSLAI TSLTNIAILF IIGLLVLTIF QISASSHLIK
PTRWNIVLET WVASILGIVK DQIGNDAKNS LIYFPLIFTF FSFVFISNIL GMIPYSFTPT
SHISVTLGLS IAIMIGVTLI GFSKHQLDFF SLFVPKGTPL ALVPLLVLIE FISYSARAFS
LALRLTANVS AGHCLFGVIS MLSVSACMAV SSILLKGITI GLPLAVLVVL YGLELLVALL
QSYVFTLLTC SYLADIVNMG DH