ID   ATP9_MARPO              Reviewed;          74 AA.
AC   P26855;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 2.
DT   02-SEP-2026, entry version 106.
DE   RecName: Full=ATP synthase subunit 9, mitochondrial;
DE   AltName: Full=Lipid-binding protein;
GN   Name=ATP9;
OS   Marchantia polymorpha (Common liverwort) (Marchantia aquatica).
OG   Mitochondrion.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=3197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A 18;
RX   PubMed=1731062; DOI=10.1016/0022-2836(92)90708-r;
RA   Oda K., Yamato K., Ohta E., Nakamura Y., Takemura M., Nozato N., Akashi K.,
RA   Kanegae T., Ogura Y., Kohchi T., Ohyama K.;
RT   "Gene organization deduced from the complete sequence of liverwort
RT   Marchantia polymorpha mitochondrial DNA. A primitive form of plant
RT   mitochondrial genome.";
RL   J. Mol. Biol. 223:1-7(1992).
CC   -!- FUNCTION: This protein is one of the chains of the nonenzymatic
CC       membrane component (F0) of mitochondrial ATPase.
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 membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000305}.
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DR   EMBL; M68929; AAC09459.1; -; Genomic_DNA.
DR   PIR; S25960; S25960.
DR   RefSeq; NP_054462.1; NC_001660.1.
DR   AlphaFoldDB; P26855; -.
DR   SMR; P26855; -.
DR   GeneID; 2702626; -.
DR   Proteomes; UP000244005; Mitochondrion.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045259; C:proton-transporting ATP synthase complex; IEA:InterPro.
DR   GO; GO:0033177; C:proton-transporting two-sector ATPase complex, proton-transporting domain; IEA:InterPro.
DR   GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
DR   CDD; cd18182; ATP-synt_Fo_c_ATP5G3; 1.
DR   FunFam; 1.20.20.10:FF:000005; ATP synthase subunit 9, mitochondrial; 1.
DR   Gene3D; 1.20.20.10; F1F0 ATP synthase subunit C; 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; ATP SYNTHASE LIPID-BINDING PROTEIN, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR10031:SF0; ATPASE PROTEIN 9; 1.
DR   Pfam; PF00137; ATP-synt_C; 1.
DR   PRINTS; PR00124; ATPASEC.
DR   SUPFAM; SSF81333; F1F0 ATP synthase subunit C; 1.
DR   PROSITE; PS00605; ATPASE_C; 1.
PE   3: Inferred from homology;
KW   ATP-binding; CF(0); Hydrogen ion transport; Ion transport; Lipid-binding;
KW   Membrane; Mitochondrion; Nucleotide-binding; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..74
FT                   /note="ATP synthase subunit 9, mitochondrial"
FT                   /id="PRO_0000112216"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        45..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   SITE            57
FT                   /note="Reversibly protonated during proton transport"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   74 AA;  7534 MW;  CA94C81A0E58F5E3 CRC64;
     MLEGAKLIGA GAATIALAGA AVGIGNVFSS LINSVARNPS LAKQLFGYAI LGFALTEAIA
     LFALMMAFLI LFVF
//