ATPA_YARLI
ID ATPA_YARLI Reviewed; 536 AA.
AC Q6C326;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=ATP synthase subunit alpha, mitochondrial {ECO:0000250|UniProtKB:P07251};
DE Flags: Precursor;
GN Name=ATP1 {ECO:0000250|UniProtKB:P07251};
GN OrderedLocusNames=YALI0_F03179g {ECO:0000312|EMBL:CAG77741.1};
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591 {ECO:0000312|Proteomes:UP000001300};
RN [1] {ECO:0000312|Proteomes:UP000001300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 25-28, IDENTIFICATION IN ATP SYNTHASE COMPLEX, FUNCTION
RP OF ATP SYNTHASE COMPLEX, SUBUNIT, SUBCELLULAR LOCATION, MASS SPECTROMETRY,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=CLIB 122 / E 150 {ECO:0000303|PubMed:25759169};
RX PubMed=25759169; DOI=10.1042/bj20150197;
RA Liu S., Charlesworth T.J., Bason J.V., Montgomery M.G., Harbour M.E.,
RA Fearnley I.M., Walker J.E.;
RT "The purification and characterization of ATP synthase complexes from the
RT mitochondria of four fungal species.";
RL Biochem. J. 468:167-175(2015).
RN [3] {ECO:0000312|PDB:5FL7}
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF ATP SYNTHASE F1C10 COMPLEX,
RP STRUCTURE BY ELECTRON MICROSCOPY (7.7 ANGSTROMS) OF DIMERIC ATP SYNTHASE
RP COMPLEX, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=27373333; DOI=10.1016/j.molcel.2016.05.037;
RA Hahn A., Parey K., Bublitz M., Mills D.J., Zickermann V., Vonck J.,
RA Kuehlbrandt W., Meier T.;
RT "Structure of a Complete ATP Synthase Dimer Reveals the Molecular Basis of
RT Inner Mitochondrial Membrane Morphology.";
RL Mol. Cell 63:445-456(2016).
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 (PubMed:25759169). F-type ATP synthases
CC consist of two structural domains, F(1) - containing the
CC extramembraneous catalytic core, and F(0) - containing the membrane
CC proton channel, linked together by a central stalk and a peripheral
CC stalk (PubMed:27373333). 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 (PubMed:27373333).
CC Subunits alpha/ATP1 and beta/ATP2 form the catalytic core in F(1)
CC (PubMed:27373333). Rotation of the central stalk against the
CC surrounding alpha/ATP1(3)beta/ATP2(3) subunits leads to hydrolysis of
CC ATP in three separate catalytic sites on the beta/ATP2 subunits
CC (PubMed:27373333). Subunit alpha/ATP1 does not bear the catalytic high-
CC affinity ATP-binding sites (PubMed:27373333).
CC {ECO:0000269|PubMed:25759169, ECO:0000269|PubMed:27373333}.
CC -!- SUBUNIT: F-type ATP synthases have 2 components, the catalytic core
CC F(1) and the membrane-embedded component F(0), linked together by a
CC central stalk and a peripheral stalk (PubMed:27373333). The central
CC stalk, also called rotor shaft, is often seen as part of F(1)
CC (PubMed:27373333). The peripheral stalk is seen as part of F(0)
CC (PubMed:27373333). F(0) contains the membrane channel next to the rotor
CC (PubMed:27373333). F-type ATP synthases form dimers but each monomer
CC functions independently in ATP generation (PubMed:27373333). The dimer
CC consists of 17 different polypeptides: ATP1 (subunit alpha, 3 molecules
CC per monomer, part of F(1)), ATP2 (subunit beta, 3 copies per monomer,
CC part of F(1)), ATP3 (subunit gamma, part of the central stalk), ATP4
CC (subunit b, part of the peripheral stalk), ATP5/OSCP (subunit 5/OSCP,
CC part of the peripheral stalk), ATP6 (subunit a, part of the peripheral
CC stalk), ATP7 (subunit d, part of the peripheral stalk), ATP8 (subunit
CC 8, part of the peripheral stalk), OLI1 (subunit c, part of the rotor,
CC 10 molecules per monomer), ATP14 (subunit h, part of the peripheral
CC stalk), ATP15 (subunit epsilon, part of the central stalk), ATP16
CC (subunit delta, part of the central stalk), ATP17 (subunit f, part of
CC the peripheral stalk), ATP18 (subunit i/j, part of the peripheral
CC stalk), ATP19 (subunit k, dimer-specific, at interface between
CC monomers), ATP20 (subunit g, at interface between monomers), TIM11
CC (subunit e, at interface between monomers) (PubMed:27373333,
CC PubMed:25759169). {ECO:0000269|PubMed:25759169,
CC ECO:0000269|PubMed:27373333}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:27373333}; Peripheral membrane protein
CC {ECO:0000305|PubMed:27373333}; Matrix side
CC {ECO:0000305|PubMed:27373333}. Note=The F-type ATP synthase complex is
CC anchored in the mitochondrial inner membrane via the F(0) domain with
CC the F(1) domain and the peripheral stalk extending into the
CC mitochondrial matrix. {ECO:0000305|PubMed:27373333}.
CC -!- MASS SPECTROMETRY: Mass=55414.9; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:25759169};
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|RuleBase:RU000339}.
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DR EMBL; CR382132; CAG77741.1; -; Genomic_DNA.
DR RefSeq; XP_504936.1; XM_504936.1.
DR PDB; 5FL7; X-ray; 3.50 A; A/B/C=1-536.
DR PDBsum; 5FL7; -.
DR AlphaFoldDB; Q6C326; -.
DR SMR; Q6C326; -.
DR STRING; 4952.CAG77741; -.
DR EnsemblFungi; CAG77741; CAG77741; YALI0_F03179g.
DR GeneID; 2907749; -.
DR KEGG; yli:YALI0F03179g; -.
DR VEuPathDB; FungiDB:YALI0_F03179g; -.
DR HOGENOM; CLU_010091_2_1_1; -.
DR InParanoid; Q6C326; -.
DR OMA; LQAPGVM; -.
DR Proteomes; UP000001300; Chromosome F.
DR GO; GO:0005754; C:mitochondrial proton-transporting ATP synthase, catalytic core; IBA:GO_Central.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
DR GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR CDD; cd18113; ATP-synt_F1_alpha_C; 1.
DR CDD; cd01132; F1_ATPase_alpha; 1.
DR Gene3D; 1.20.150.20; -; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01346; ATP_synth_alpha_bact; 1.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR000793; ATP_synth_asu_C.
DR InterPro; IPR038376; ATP_synth_asu_C_sf.
DR InterPro; IPR033732; ATP_synth_F1_a.
DR InterPro; IPR005294; ATP_synth_F1_asu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF00306; ATP-synt_ab_C; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00962; atpA; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; ATP-binding; CF(1); Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Reference proteome;
KW Transit peptide; Transport.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25759169"
FT CHAIN 25..536
FT /note="ATP synthase subunit alpha, mitochondrial"
FT /evidence="ECO:0000305"
FT /id="PRO_0000445310"
FT BINDING 195..202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27373333,
FT ECO:0007744|PDB:5FL7"
FT STRAND 52..61
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 177..182
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 201..211
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:5FL7"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 226..233
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 236..247
FT /evidence="ECO:0007829|PDB:5FL7"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 266..285
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 289..295
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 298..310
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 325..332
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 346..354
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 363..369
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 372..378
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 380..385
FT /evidence="ECO:0007829|PDB:5FL7"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:5FL7"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 414..419
FT /evidence="ECO:0007829|PDB:5FL7"
FT TURN 420..423
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 424..428
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 429..432
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 438..453
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 464..476
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 478..482
FT /evidence="ECO:0007829|PDB:5FL7"
FT TURN 484..486
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 487..492
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 495..501
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 503..509
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 517..527
FT /evidence="ECO:0007829|PDB:5FL7"
SQ SEQUENCE 536 AA; 58079 MW; C67EB8201B885E49 CRC64;
MFKNALRRAG VAAPRISRVA QRGYAEAKAT PTEVTSILEE RIRGVSGEAN LNETGRVLSV
GDGIARVFGL NNIQAEELVE FASGVKGMAL NLEAGQVGIV LFGSDRLVKE GETVKRSGSI
VDVPVGPALL GRVVDALGNP IDGKGPIETE FRIRAQVKAP GILPRTSVNE PMQTGLKAVD
ALVPIGRGQR ELIIGDRQTG KTQIAIDTIL NQKRWNYGQD EKKKLYCVYV AVGQKRSTVA
QLVQTLEHHD ALKYSIIVAA TASEAAPLQY LAPFTGTAMG EWFRDNGKGA LIVFDDLSKQ
AVAYRQMSLL LRRPPGREAY PGDVFYLHSR LLERAAKMNE REGGGSLTAL PIIETQGGDV
SAYIPTNVIS ITDGQIFLEA ELFYKGIRPA INVGLSVSRV GSAAQVKAMK QVAGSLKLFL
AQYREVAAFA QFGSDLDAST KQTLTRGERL TLLLKQKQAS PMSSEEMVPL IYAGVNGYID
NIPVKQVEKF EAEFVSYLHA NESDLLKDIA ATGELSKENL EKLKSITENF VGSFAK
