ID   ATP6_SOLTU              Reviewed;          55 AA.
AC   P80497; M1A649;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-FEB-2022, sequence version 2.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=ATP synthase small subunit 6, mitochondrial {ECO:0000305};
DE            Short=MtATP6 {ECO:0000305};
DE   AltName: Full=ATP synthase 6 kDa subunit, mitochondrial {ECO:0000303|PubMed:8919912};
DE   Flags: Precursor;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DM1-3 516 R44;
RX   PubMed=21743474; DOI=10.1038/nature10158;
RG   The Potato Genome Sequencing Consortium;
RT   "Genome sequence and analysis of the tuber crop potato.";
RL   Nature 475:189-195(2011).
RN   [2]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Tuber;
RX   PubMed=8919912; DOI=10.1046/j.1365-313x.1996.09030357.x;
RA   Jansch L., Kruft V., Schmitz U.K., Braun H.P.;
RT   "New insights into the composition, molecular mass and stoichiometry of the
RT   protein complexes of plant mitochondria.";
RL   Plant J. 9:357-368(1996).
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 (Probable). F-type ATPases consist of two
CC       structural domains, F(1) - containing the extramembraneous catalytic
CC       core and F(0) - containing the membrane proton channel, linked together
CC       by a central stalk and a peripheral stalk (Probable). During catalysis,
CC       ATP synthesis in the catalytic domain of F(1) is coupled via a rotary
CC       mechanism of the central stalk subunits to proton translocation
CC       (Probable). Part of the complex F(0) domain (Probable). Confers
CC       tolerance to several abiotic stresses (e.g. salt, mannitol, drought,
CC       oxidative and cold stresses), probably by providing additional energy
CC       needed for cell homeostasis (By similarity).
CC       {ECO:0000250|UniProtKB:P0DO44, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P0DO44}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the ATPase 6 subunit family. {ECO:0000305}.
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DR   STRING; 4113.PGSC0003DMT400015500; -.
DR   eggNOG; ENOG502S6YY; Eukaryota.
DR   HOGENOM; CLU_200132_0_0_1; -.
DR   OMA; TWPFIAG; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   CF(0); Direct protein sequencing; Hydrogen ion transport; Ion transport;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Stress response; Transit peptide; Transmembrane; Transmembrane helix;
KW   Transport.
FT   TRANSIT         1..15
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..55
FT                   /note="ATP synthase small subunit 6, mitochondrial"
FT                   /id="PRO_0000071723"
FT   TRANSMEM        20..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        19
FT                   /note="W -> Q (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   55 AA;  6705 MW;  9A9D176C2A8AA3EE CRC64;
     MRQFDPWPVF FRREWSRNWP FLVGFAVTGA IITKMSLGFT EEERKNSRFA QRHKN