ATP9_YARLI
ID ATP9_YARLI Reviewed; 76 AA.
AC Q37695;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=ATP synthase subunit 9, mitochondrial {ECO:0000250|UniProtKB:P61829};
DE AltName: Full=ATP synthase subunit c {ECO:0000303|PubMed:25759169};
DE AltName: Full=Lipid-binding protein {ECO:0000250|UniProtKB:P61829};
GN Name=OLI1 {ECO:0000250|UniProtKB:P61829};
GN Synonyms=ATP9 {ECO:0000250|UniProtKB:P61829};
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 44601 / 281;
RX PubMed=7533057; DOI=10.1007/bf00309923;
RA Matsuoka M., Matsubara M., Inoue J., Kakehi M., Imanaka T.;
RT "Organization and transcription of the mitochondrial ATP synthase genes in
RT the yeast Yarrowia lipolytica.";
RL Curr. Genet. 26:382-389(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20460 / W29 / CBS 7504 / IFP29;
RX DOI=10.1002/cfg.72;
RA Kerscher S., Durstewitz G., Casaregola S., Gaillardin C., Brandt U.;
RT "The complete mitochondrial genome of Yarrowia lipolytica.";
RL Comp. Funct. Genomics 2:80-90(2001).
RN [3]
RP PROTEIN SEQUENCE OF 1-9, IDENTIFICATION IN ATP SYNTHASE COMPLEX, FUNCTION
RP OF ATP SYNTHASE COMPLEX, SUBUNIT, SUBCELLULAR LOCATION, MASS SPECTROMETRY,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND FORMYLATION AT MET-1.
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 [4]
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, AND SUBCELLULAR LOCATION.
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(0) domain. A homomeric c-ring of 10 OLI1/ATP9 subunits
CC is part of the complex rotary element (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}; Multi-pass membrane protein
CC {ECO:0000255}. Note=The F-type ATP synthase complex is anchored in the
CC mitochondrial inner membrane via the F(0) domain with the F(1) domain
CC and the peripheral stalk extending into the mitochondrial matrix.
CC {ECO:0000305|PubMed:27373333}.
CC -!- MASS SPECTROMETRY: Mass=7744.6; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:25759169};
CC -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000305}.
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DR EMBL; L15359; AAA78262.1; -; Genomic_DNA.
DR EMBL; AJ307410; CAC28104.1; -; Genomic_DNA.
DR PIR; S51504; S51504.
DR RefSeq; NP_075437.1; NC_002659.1.
DR PDB; 5FL7; X-ray; 3.50 A; K/L/M/N/O/P/Q/R/S/T=1-76.
DR PDBsum; 5FL7; -.
DR AlphaFoldDB; Q37695; -.
DR SMR; Q37695; -.
DR STRING; 284591.Q37695; -.
DR GeneID; 802622; -.
DR KEGG; yli:YalifMp17; -.
DR InParanoid; Q37695; -.
DR Proteomes; UP000001300; 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); IBA:GO_Central.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR Gene3D; 1.20.20.10; -; 1.
DR HAMAP; MF_01396; ATP_synth_c_bact; 1.
DR InterPro; IPR000454; ATP_synth_F0_csu.
DR InterPro; IPR020537; ATP_synth_F0_csu_DDCD_BS.
DR InterPro; IPR038662; ATP_synth_F0_csu_sf.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR PANTHER; PTHR10031; PTHR10031; 1.
DR Pfam; PF00137; ATP-synt_C; 1.
DR PRINTS; PR00124; ATPASEC.
DR SUPFAM; SSF81333; SSF81333; 1.
DR PROSITE; PS00605; ATPASE_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; CF(0); Direct protein sequencing; Formylation;
KW Hydrogen ion transport; Ion transport; Lipid-binding; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..76
FT /note="ATP synthase subunit 9, mitochondrial"
FT /id="PRO_0000112239"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 59
FT /note="Reversibly protonated during proton transport"
FT /evidence="ECO:0000305|PubMed:27373333"
FT MOD_RES 1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000269|PubMed:7533057"
FT HELIX 3..15
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 19..37
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:5FL7"
FT HELIX 44..73
FT /evidence="ECO:0007829|PDB:5FL7"
SQ SEQUENCE 76 AA; 7716 MW; 9CB58665025AC10B CRC64;
MQLVLAGKYI GAGLASIGLV GAGIGIAIVF AALINGVSRN PALKGQLFTY SILGFALSEA
TGLFALMIAF LLLYAV
