ATP9_TRIRU
ID ATP9_TRIRU Reviewed; 74 AA.
AC Q01554;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=ATP synthase subunit 9, mitochondrial;
DE AltName: Full=Lipid-binding protein;
GN Name=ATP9;
OS Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=5551;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IP 1817.89;
RX PubMed=1326416; DOI=10.1007/bf00351730;
RA de Bievre C., Dujon B.;
RT "Mitochondrial DNA sequence analysis of the cytochrome oxidase subunit I
RT and II genes, the ATPase9 gene, the NADH dehydrogenase ND4L and ND5 gene
RT complex, and the glutaminyl, methionyl and arginyl tRNA genes from
RT Trichophyton rubrum.";
RL Curr. Genet. 22:229-234(1992).
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.
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; X65223; CAA46326.1; -; Genomic_DNA.
DR PIR; S26943; S26943.
DR AlphaFoldDB; Q01554; -.
DR SMR; Q01554; -.
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_0000112236"
FT TRANSMEM 16..36
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"
SQ SEQUENCE 74 AA; 7492 MW; AE01C45FD7E9E681 CRC64;
MIQAAKIIGT GLATTGLIGA GVGIGVVFGA LILGVARNPS LRGLLFSYAI LGFAFSEATG
LFALMMAFLL LYVA