ATP9_BETVU
ID ATP9_BETVU Reviewed; 88 AA.
AC P14571;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=ATP synthase subunit 9, mitochondrial;
DE EC=7.1.2.2;
DE AltName: Full=Lipid-binding protein;
GN Name=ATP9;
OS Beta vulgaris (Sugar beet).
OG Mitochondrion.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Betoideae; Beta.
OX NCBI_TaxID=161934;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2531368; DOI=10.1093/nar/17.21.8857;
RA Xue Y., Thomas C.M., Davies D.R.;
RT "Nucleotide sequence and transcription of the sugar beet mitochondrial
RT F0F1-ATPase subunit 9 gene.";
RL Nucleic Acids Res. 17:8857-8857(1989).
CC -!- FUNCTION: This protein is one of the chains of the nonenzymatic
CC membrane component (F0) of mitochondrial ATPase.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
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; X16593; CAA34604.1; -; Genomic_DNA.
DR PIR; S14907; LWET9.
DR AlphaFoldDB; P14571; -.
DR SMR; P14571; -.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
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 ATP-binding; CF(0); Hydrogen ion transport; Ion transport; Lipid-binding;
KW Membrane; Mitochondrion; Nucleotide-binding; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..88
FT /note="ATP synthase subunit 9, mitochondrial"
FT /id="PRO_0000112209"
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 88 AA; 9007 MW; 1798403BF39F9F89 CRC64;
MLEGAKSIGA GAATIASAGA AIGIGNVFSS LIHSVARNPS LAKQLFGYAI LGFALSELIA
LFALMMAFLI LFAFRFFSKK GKLAGAPV
