ATPG_YARLI
ID ATPG_YARLI Reviewed; 293 AA.
AC Q6C338;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=ATP synthase subunit gamma, mitochondrial {ECO:0000250|UniProtKB:P38077};
DE AltName: Full=F-ATPase gamma subunit {ECO:0000250|UniProtKB:P38077};
DE Flags: Precursor;
GN Name=ATP3 {ECO:0000250|UniProtKB:P38077};
GN OrderedLocusNames=YALI0_F02893g {ECO:0000312|EMBL:CAG77729.2};
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 IDENTIFICATION IN ATP SYNTHASE COMPLEX, FUNCTION OF ATP SYNTHASE COMPLEX,
RP SUBUNIT, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND IDENTIFICATION BY
RP 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:0000305}
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). Part
CC of the complex F(1) domain and the central stalk which is part of the
CC complex rotary element (PubMed:27373333). The gamma/ATP3 subunit
CC protrudes into the catalytic domain formed of alpha/ATP1(3)beta/ATP2(3)
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). {ECO:0000269|PubMed:25759169,
CC 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=30077.2; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:25759169};
CC -!- SIMILARITY: Belongs to the ATPase gamma chain family.
CC {ECO:0000255|RuleBase:RU004001}.
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DR EMBL; CR382132; CAG77729.2; -; Genomic_DNA.
DR RefSeq; XP_504924.2; XM_504924.2.
DR PDB; 5FL7; X-ray; 3.50 A; G=1-293.
DR PDBsum; 5FL7; -.
DR AlphaFoldDB; Q6C338; -.
DR SMR; Q6C338; -.
DR STRING; 4952.CAG77729; -.
DR EnsemblFungi; CAG77729; CAG77729; YALI0_F02893g.
DR GeneID; 2907762; -.
DR KEGG; yli:YALI0F02893g; -.
DR VEuPathDB; FungiDB:YALI0_F02893g; -.
DR HOGENOM; CLU_050669_4_1_1; -.
DR InParanoid; Q6C338; -.
DR OMA; MQITSAM; -.
DR Proteomes; UP000001300; Chromosome F.
DR GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); IBA:GO_Central.
DR GO; GO:0005756; C:mitochondrial proton-transporting ATP synthase, central stalk; IEA:EnsemblFungi.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:EnsemblFungi.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:EnsemblFungi.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR CDD; cd12151; F1-ATPase_gamma; 1.
DR InterPro; IPR035968; ATP_synth_F1_ATPase_gsu.
DR InterPro; IPR000131; ATP_synth_F1_gsu.
DR InterPro; IPR023632; ATP_synth_F1_gsu_CS.
DR PANTHER; PTHR11693; PTHR11693; 1.
DR Pfam; PF00231; ATP-synt; 1.
DR PRINTS; PR00126; ATPASEGAMMA.
DR SUPFAM; SSF52943; SSF52943; 1.
DR TIGRFAMs; TIGR01146; ATPsyn_F1gamma; 1.
DR PROSITE; PS00153; ATPASE_GAMMA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; CF(1); Hydrogen ion transport; Ion transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transit peptide; Transport.
FT TRANSIT 1..21
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25759169"
FT CHAIN 22..293
FT /note="ATP synthase subunit gamma, mitochondrial"
FT /evidence="ECO:0000305"
FT /id="PRO_0000445318"
FT HELIX 25..42
FT /evidence="ECO:0007829|PDB:5FL7"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 46..63
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:5FL7"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 102..115
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 131..137
FT /evidence="ECO:0007829|PDB:5FL7"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 160..172
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:5FL7"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 202..206
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 223..289
FT /evidence="ECO:0007829|PDB:5FL7"
SQ SEQUENCE 293 AA; 32337 MW; 8EEBF65F211CB2AD CRC64;
MFALRTAARP AARSVGATRN YATLREIEMR LKSIKNIEKI TNTMKIVAST KLGKAQRAMA
TSKVYNEASE KVFENSETAV PENIEKRLWV VVSSDKGLCG SIHSQLARTV RRKLLDFESG
EKLIDIVAVG EKIKAQLGRS NPEQMRLSFG GTGKEAPTFE EAAHIADEIL ALDTQYDDIE
IVYNKVLSGI SFEPIMKESY SAKAIEDAPK FGQYELEDDV VKNLADFSLA NTIYAAMAEG
HAAEISARRN AMDNASKNAS DMINKYSILY NRTRQAVITN ELVDIITGAS SLE
