ATP6_CANPA
ID ATP6_CANPA Reviewed; 246 AA.
AC Q03671;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=ATP synthase subunit a;
DE AltName: Full=ATP synthase subunit 6;
DE AltName: Full=F-ATPase protein 6;
DE Flags: Precursor;
GN Name=ATP6; Synonyms=OLI2;
OS Candida parapsilosis (Yeast).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5480;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 4-25.
RC STRAIN=CBS 7154 / SP1;
RX PubMed=1826652; DOI=10.1111/j.1432-1033.1991.tb15887.x;
RA Guelin E., Guerin M., Velours J.;
RT "Isolation of the ATP synthase subunit 6 and sequence of the mitochondrial
RT ATP6 gene of the yeast Candida parapsilosis.";
RL Eur. J. Biochem. 197:105-111(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SR23 / CBS 7157;
RX PubMed=15449175; DOI=10.1007/s00438-004-1046-0;
RA Nosek J., Novotna M., Hlavatovicova Z., Ussery D.W., Fajkus J., Tomaska L.;
RT "Complete DNA sequence of the linear mitochondrial genome of the pathogenic
RT yeast Candida parapsilosis.";
RL Mol. Genet. Genomics 272:173-180(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 228-246.
RC STRAIN=SR23 / CBS 7157;
RX PubMed=7715605; DOI=10.1007/bf00425822;
RA Nosek J., Dinouel N., Kovac L., Fukuhara H.;
RT "Linear mitochondrial DNAs from yeasts: telomeres with large tandem
RT repetitions.";
RL Mol. Gen. Genet. 247:61-72(1995).
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; X55653; CAA39185.1; -; Genomic_DNA.
DR EMBL; X74411; CAE54611.1; -; Genomic_DNA.
DR PIR; S15378; S15378.
DR RefSeq; NP_943649.1; NC_005253.2.
DR AlphaFoldDB; Q03671; -.
DR SMR; Q03671; -.
DR GeneID; 2657765; -.
DR VEuPathDB; FungiDB:CapafMp17; -.
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); IEA:EnsemblFungi.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:EnsemblFungi.
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 1: Evidence at protein level;
KW ATP synthesis; CF(0); Direct protein sequencing; Hydrogen ion transport;
KW Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Transmembrane; Transmembrane helix; Transport.
FT PROPEP 1..3
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:1826652"
FT /id="PRO_0000002610"
FT CHAIN 4..246
FT /note="ATP synthase subunit a"
FT /id="PRO_0000002611"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 74
FT /note="Q -> P (in Ref. 1; CAA39185)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 246 AA; 26980 MW; D3DC1BED83D63F82 CRC64;
MFYSPLDQFE LKPLLLITDN LTFSITNYTL YLIIVSLIII FYSSIIRHNY LGSSRWGVSV
IAIYDTILNL VNGQIGRKGG YYFPLIFTIF NFILIANLIS MIPYSFAISA QLVAVVSFSL
TLWIGNVVLG LYLHGWGFFA LFVPSGTPLA LVPVLVLIEA LSYASRAISL GLRLGANILS
GHLLMLILGS LIISLMSSSF LGFVSGIIPI LAVVAITILE FGIAIIQAYV FSILLSGYIK
DSVELH
