ATP6_YEAST
ID ATP6_YEAST Reviewed; 259 AA.
AC P00854; A0A0A7P052; Q95A27;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=ATP synthase subunit a;
DE AltName: Full=F-ATPase protein 6;
DE Flags: Precursor;
GN Name=ATP6; Synonyms=OLI2, OLI4, PHO1; OrderedLocusNames=Q0085;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=D273-10B/A1;
RX PubMed=6446405; DOI=10.1016/0092-8674(80)90637-6;
RA Macino G., Tzagoloff A.;
RT "Assembly of the mitochondrial membrane system: sequence analysis of a
RT yeast mitochondrial ATPase gene containing the oli-2 and oli-4 loci.";
RL Cell 20:507-517(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JM6;
RX PubMed=2950378; DOI=10.1093/nar/15.1.366;
RA John U.P., Nagley P.;
RT "Sequence of the mitochondrial oli2 gene coding for subunit 6 of the
RT mitochondrial ATPase complex in different strains of Saccharomyces.";
RL Nucleic Acids Res. 15:366-366(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9872396; DOI=10.1016/s0014-5793(98)01467-7;
RA Foury F., Roganti T., Lecrenier N., Purnelle B.;
RT "The complete sequence of the mitochondrial genome of Saccharomyces
RT cerevisiae.";
RL FEBS Lett. 440:325-331(1998).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP PROTEIN SEQUENCE OF 11-32.
RX PubMed=2894987; DOI=10.1111/j.1432-1033.1988.tb13934.x;
RA Michon T., Galante M., Velours J.;
RT "NH2-terminal sequence of the isolated yeast ATP synthase subunit 6 reveals
RT post-translational cleavage.";
RL Eur. J. Biochem. 172:621-625(1988).
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. In yeast, the dimeric form
CC of ATP synthase consists of 17 polypeptides: alpha, beta, gamma, delta,
CC epsilon, 4 (B), 5 (OSCP), 6 (A), 8, 9 (C), d, E (Tim11), f, g, h, i/j
CC and k.
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; J01464; AAA32145.2; -; Genomic_DNA.
DR EMBL; V00683; CAA24054.1; -; Genomic_DNA.
DR EMBL; X05056; CAA28727.1; -; Genomic_DNA.
DR EMBL; KP263414; AIZ98889.1; -; Genomic_DNA.
DR PIR; A25869; PWBYJ6.
DR RefSeq; NP_009313.1; NC_001224.1.
DR PDB; 6B2Z; EM; 3.60 A; M/a=11-259.
DR PDB; 6B8H; EM; 3.60 A; a/p=11-259.
DR PDB; 6CP3; EM; 3.80 A; X=11-259.
DR PDB; 6CP5; EM; 4.20 A; X=11-259.
DR PDB; 6CP6; EM; 3.60 A; X=11-259.
DR PDB; 6CP7; EM; 4.10 A; X=11-259.
DR PDB; 6WTD; EM; 4.20 A; X=11-259.
DR PDBsum; 6B2Z; -.
DR PDBsum; 6B8H; -.
DR PDBsum; 6CP3; -.
DR PDBsum; 6CP5; -.
DR PDBsum; 6CP6; -.
DR PDBsum; 6CP7; -.
DR PDBsum; 6WTD; -.
DR AlphaFoldDB; P00854; -.
DR SMR; P00854; -.
DR BioGRID; 34793; 28.
DR ComplexPortal; CPX-3281; Mitochondrial proton-transporting ATP synthase complex.
DR DIP; DIP-3038N; -.
DR IntAct; P00854; 2.
DR STRING; 4932.Q0085; -.
DR TCDB; 3.A.2.1.3; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR PaxDb; P00854; -.
DR PRIDE; P00854; -.
DR EnsemblFungi; Q0085_mRNA; Q0085; Q0085.
DR GeneID; 854601; -.
DR KEGG; sce:Q0085; -.
DR SGD; S000007268; ATP6.
DR VEuPathDB; FungiDB:Q0085; -.
DR eggNOG; KOG4665; Eukaryota.
DR GeneTree; ENSGT00390000005568; -.
DR HOGENOM; CLU_041018_0_2_1; -.
DR InParanoid; P00854; -.
DR OMA; FFDQFMS; -.
DR BioCyc; YEAST:G3O-34379-MON; -.
DR Reactome; R-SCE-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-SCE-8949613; Cristae formation.
DR PRO; PR:P00854; -.
DR Proteomes; UP000002311; Mitochondrion.
DR RNAct; P00854; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IC:ComplexPortal.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IDA:SGD.
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 3D-structure; ATP synthesis; CF(0); Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT PROPEP 1..10
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:2894987"
FT /id="PRO_0000002626"
FT CHAIN 11..259
FT /note="ATP synthase subunit a"
FT /id="PRO_0000002627"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VARIANT 171
FT /note="I -> M (in strain: D273-10B/A1)"
FT VARIANT 177
FT /note="F -> I (in strain: D273-10B/A1)"
FT VARIANT 231
FT /note="M -> I (in strain: D273-10B/A1)"
FT VARIANT 241
FT /note="G -> S (in strain: D273-10B/A1)"
FT VARIANT 245
FT /note="A -> T (in strain: D273-10B/A1)"
FT VARIANT 255..256
FT /note="AV -> TL (in strain: D273-10B/A1)"
SQ SEQUENCE 259 AA; 29099 MW; 1A3257747B5A7C57 CRC64;
MFNLLNTYIT SPLDQFEIRT LFGLQSSFID LSCLNLTTFS LYTIIVLLVI TSLYTLTNNN
NKIIGSRWLI SQEAIYDTIM NMTKGQIGGK NWGLYFPMIF TLFMFIFIAN LISMIPYSFA
LSAHLVFIIS LSIVIWLGNT ILGLYKHGWV FFSLFVPAGT PLPLVPLLVI IETLSYFARA
ISLGLRLGSN ILAGHLLMVI LAGLTFNFML INLFTLVFGF VPLAMILAIM MLEFAIGIIQ
GYVWAILTAS YLKDAVYLH
