ATP9_ACACA
ID ATP9_ACACA Reviewed; 79 AA.
AC Q37377;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=ATP synthase subunit 9, mitochondrial;
DE AltName: Full=Lipid-binding protein;
GN Name=ATP9;
OS Acanthamoeba castellanii (Amoeba).
OG Mitochondrion.
OC Eukaryota; Amoebozoa; Discosea; Longamoebia; Centramoebida;
OC Acanthamoebidae; Acanthamoeba.
OX NCBI_TaxID=5755;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 30010 / Neff;
RX PubMed=7844823; DOI=10.1006/jmbi.1994.0043;
RA Burger G., Plante I., Lonergan K.M., Gray M.W.;
RT "The mitochondrial DNA of the amoeboid protozoon, Acanthamoeba castellanii:
RT complete sequence, gene content and genome organization.";
RL J. Mol. Biol. 245:522-537(1995).
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; U12386; AAD11829.1; -; Genomic_DNA.
DR PIR; S53837; S53837.
DR RefSeq; NP_042536.1; NC_001637.1.
DR AlphaFoldDB; Q37377; -.
DR SMR; Q37377; -.
DR GeneID; 1734033; -.
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..79
FT /note="ATP synthase subunit 9, mitochondrial"
FT /id="PRO_0000112227"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 63
FT /note="Reversibly protonated during proton transport"
FT /evidence="ECO:0000250"
SQ SEQUENCE 79 AA; 8246 MW; D114D06E18C3AC26 CRC64;
MKNLEIILQS SKMIGSGLAT SGLIGAGAGV GIVFGCLILA FSRNPNLQKE LFSYALIGFA
LTEAIGLLAL VMAFLILFI
