ID   YMF19_RAPSA             Reviewed;         158 AA.
AC   Q06564;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Putative ATP synthase protein YMF19;
DE            EC=7.1.2.2;
DE   AltName: Full=Mitochondrial protein YMF19;
GN   Name=YMF19;
OS   Raphanus sativus (Radish) (Raphanus raphanistrum var. sativus).
OG   Mitochondrion.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Raphanus.
OX   NCBI_TaxID=3726;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Scarlet Knight; TISSUE=Green leaf;
RX   PubMed=8358822; DOI=10.1007/bf00324680;
RA   Krishnasamy S., Makaroff C.A.;
RT   "Characterization of the radish mitochondrial orfB locus: possible
RT   relationship with male sterility in Ogura radish.";
RL   Curr. Genet. 24:156-163(1993).
CC   -!- FUNCTION: This is one of the chains of the nonenzymatic component
CC       (CF(0) subunit) of the mitochondrial ATPase complex. {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Single-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATPase protein YMF19 family. {ECO:0000305}.
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DR   EMBL; Z18895; CAA79331.1; -; Genomic_DNA.
DR   EMBL; Z18896; CAA79333.1; -; Genomic_DNA.
DR   PIR; S33916; S33916.
DR   RefSeq; YP_006665999.1; NC_018551.1.
DR   AlphaFoldDB; Q06564; -.
DR   SMR; Q06564; -.
DR   GeneID; 13630173; -.
DR   KEGG; rsz:13630173; -.
DR   OrthoDB; 1310286at2759; -.
DR   Proteomes; UP000504610; Mitochondrion MT.
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: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   InterPro; IPR009455; YMF19.
DR   InterPro; IPR044975; YMF19-like.
DR   InterPro; IPR003319; YMF19-like_N.
DR   PANTHER; PTHR36816; PTHR36816; 1.
DR   Pfam; PF06449; DUF1082; 1.
DR   Pfam; PF02326; YMF19; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; ATP-binding; CF(0); Hydrogen ion transport; Ion transport;
KW   Membrane; Mitochondrion; Nucleotide-binding; Reference proteome;
KW   Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..158
FT                   /note="Putative ATP synthase protein YMF19"
FT                   /id="PRO_0000196844"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   VARIANT         124
FT                   /note="I -> L (in Ogura, male-sterile line)"
SQ   SEQUENCE   158 AA;  18155 MW;  0A895BA7F998B656 CRC64;
     MPQLDKFTYF SQFFWLCLFF FTFYIFICND GDGVLGISRI LKLRNQLLSH RGKTIQSKDP
     NSLEDLLRKG FSTGVSYMYA SLFEVSQWCK AVDLLGKRRK ITLISCFGEI SGSRGMERNI
     LYNISKSSPS NTGRWITCRN CRNDIMLIHA VHGQGSIK