ID   ATP9_RHIOR              Reviewed;          74 AA.
AC   Q3T4E5;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=ATP synthase subunit 9, mitochondrial {ECO:0000250|UniProtKB:P61829};
DE   AltName: Full=Lipid-binding protein {ECO:0000250|UniProtKB:P61829};
GN   Name=atp9 {ECO:0000312|EMBL:AAW49478.1};
OS   Rhizopus oryzae (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OG   Mitochondrion {ECO:0000312|EMBL:AAW49478.1}.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=64495;
RN   [1] {ECO:0000312|EMBL:AAW49478.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DAOM 148428 {ECO:0000312|EMBL:AAW49478.1};
RX   PubMed=15689432; DOI=10.1093/nar/gki199;
RA   Seif E., Leigh J., Liu Y., Roewer I., Forget L., Lang B.F.;
RT   "Comparative mitochondrial genomics in zygomycetes: bacteria-like RNase P
RT   RNAs, mobile elements, and a close source of the group I intron invasion in
RT   angiosperms.";
RL   Nucleic Acids Res. 33:734-744(2005).
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. Part of the complex
CC       F(0) domain. A homomeric c-ring of probably 10 subunits is part of the
CC       complex rotary element. {ECO:0000305}.
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. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000255}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000255}.
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DR   EMBL; AY863212; AAW49478.1; -; Genomic_DNA.
DR   RefSeq; YP_203311.1; NC_006836.1.
DR   AlphaFoldDB; Q3T4E5; -.
DR   SMR; Q3T4E5; -.
DR   GeneID; 3260161; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
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; IEA:InterPro.
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   3: Inferred from homology;
KW   CF(0); Hydrogen ion transport; Ion transport; Lipid-binding; Membrane;
KW   Mitochondrion; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..74
FT                   /note="ATP synthase subunit 9, mitochondrial"
FT                   /id="PRO_0000391439"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   SITE            57
FT                   /note="Reversibly protonated during proton transport"
FT                   /evidence="ECO:0000250|UniProtKB:P00845"
SQ   SEQUENCE   74 AA;  7473 MW;  83FE51CC2FFBBE50 CRC64;
     MVAAAKILGA GLATIGLAGA GVGVGLVFAA LINSTSRNPS LRPQLFSYTI LGFALTEAIG
     LFALMMAFLL LYAA