ATP8_CANGA
ID ATP8_CANGA Reviewed; 48 AA.
AC P05040;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=ATP synthase protein 8;
DE AltName: Full=A6L;
DE AltName: Full=F-ATPase subunit 8;
GN Name=ATP8;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=4040462; DOI=10.1002/j.1460-2075.1985.tb03652.x;
RA Clark-Walker G.D., McArthur C.R., Sriprakash K.S.;
RT "Location of transcriptional control signals and transfer RNA sequences in
RT Torulopsis glabrata mitochondrial DNA.";
RL EMBO J. 4:465-473(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=12527359; DOI=10.1016/s0014-5793(02)03749-3;
RA Koszul R., Malpertuy A., Frangeul L., Bouchier C., Wincker P., Thierry A.,
RA Duthoy S., Ferris S., Hennequin C., Dujon B.;
RT "The complete mitochondrial genome sequence of the pathogenic yeast Candida
RT (Torulopsis) glabrata.";
RL FEBS Lett. 534:39-48(2003).
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. Part of the complex
CC F(0) domain. Minor subunit located with subunit a in the membrane (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the ATPase protein 8 family. {ECO:0000305}.
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DR EMBL; X02169; CAA26110.1; -; Genomic_DNA.
DR EMBL; AJ511533; CAD54423.1; -; Genomic_DNA.
DR PIR; S07188; S07188.
DR RefSeq; NP_818782.1; NC_004691.1.
DR AlphaFoldDB; P05040; -.
DR SMR; P05040; -.
DR STRING; 284593.P05040; -.
DR GeneID; 807005; -.
DR KEGG; cgr:CaglfMp08; -.
DR CGD; CAL0139462; ATP8.
DR VEuPathDB; FungiDB:CaglfMp08; -.
DR InParanoid; P05040; -.
DR Proteomes; UP000002428; Mitochondrion.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); ISO:CGD.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:EnsemblFungi.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; ISO:CGD.
DR InterPro; IPR009230; ATP_synth_su8_fun.
DR Pfam; PF05933; Fun_ATP-synt_8; 1.
PE 3: Inferred from homology;
KW ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW Mitochondrion; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..48
FT /note="ATP synthase protein 8"
FT /id="PRO_0000195597"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 48 AA; 5770 MW; 90B46140BFA673C8 CRC64;
MPQLIPFYFM NQLTYGLLLI TVLLILFSQF FLPMILRLYV SRLFISKL
