ID   ATPG3_IPOBA             Reviewed;         326 AA.
AC   P26360;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=ATP synthase subunit gamma, mitochondrial;
DE   AltName: Full=F-ATPase gamma subunit;
DE   Flags: Precursor;
GN   Name=ATPC;
OS   Ipomoea batatas (Sweet potato) (Convolvulus batatas).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
OX   NCBI_TaxID=4120;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Kokei No. 14; TISSUE=Tuberous root;
RX   PubMed=8349605; DOI=10.1016/s0021-9258(19)85323-1;
RA   Morikami A., Ehara G., Yuuki K., Nakamura K.;
RT   "Molecular cloning and characterization of cDNAs for the gamma- and
RT   epsilon-subunits of mitochondrial F1F0 ATP synthase from the sweet
RT   potato.";
RL   J. Biol. Chem. 268:17205-17210(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 46-80.
RC   STRAIN=cv. Kokei No. 14; TISSUE=Tuberous root;
RX   PubMed=2536736; DOI=10.1016/s0021-9258(18)94048-2;
RA   Kimura T., Nakamura K., Kajiura H., Hattori H., Nelson N., Asahi T.;
RT   "Correspondence of minor subunits of plant mitochondrial F1ATPase to
RT   F1F0ATPase subunits of other organisms.";
RL   J. Biol. Chem. 264:3183-3186(1989).
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
CC       F(0) - containing the membrane proton channel, linked together by a
CC       central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC       in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC       the central stalk subunits to proton translocation. Part of the complex
CC       F(1) domain and the central stalk which is part of the complex rotary
CC       element. The gamma subunit protrudes into the catalytic domain formed
CC       of alpha(3)beta(3). Rotation of the central stalk against the
CC       surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in
CC       three separate catalytic sites on the beta subunits.
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. Mitochondrion inner membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATPase gamma chain family. {ECO:0000305}.
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DR   EMBL; D14699; BAA03526.1; -; mRNA.
DR   PIR; A47493; A47493.
DR   AlphaFoldDB; P26360; -.
DR   SMR; P26360; -.
DR   PRIDE; P26360; -.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR   CDD; cd12151; F1-ATPase_gamma; 1.
DR   HAMAP; MF_00815; ATP_synth_gamma_bact; 1.
DR   InterPro; IPR035968; ATP_synth_F1_ATPase_gsu.
DR   InterPro; IPR000131; ATP_synth_F1_gsu.
DR   InterPro; IPR023632; ATP_synth_F1_gsu_CS.
DR   PANTHER; PTHR11693; PTHR11693; 1.
DR   Pfam; PF00231; ATP-synt; 1.
DR   PRINTS; PR00126; ATPASEGAMMA.
DR   SUPFAM; SSF52943; SSF52943; 1.
DR   TIGRFAMs; TIGR01146; ATPsyn_F1gamma; 1.
DR   PROSITE; PS00153; ATPASE_GAMMA; 1.
PE   1: Evidence at protein level;
KW   ATP synthesis; CF(1); Direct protein sequencing; Hydrogen ion transport;
KW   Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Transit peptide; Transport.
FT   TRANSIT         1..45
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:2536736"
FT   CHAIN           46..326
FT                   /note="ATP synthase subunit gamma, mitochondrial"
FT                   /id="PRO_0000002683"
FT   CONFLICT        65..66
FT                   /note="TK -> IS (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        74
FT                   /note="S -> A (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        80
FT                   /note="Q -> N (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   326 AA;  35576 MW;  550982D9E1595813 CRC64;
     MAMAALRREG RRLAAAPFTS PTPLNALRSS LVSPSEEIGL SGVRSISTQV VRNRMKSVKN
     IQKITKAMKM VAASKLRAIQ TRAENSRGLW QPFTALLGDT PSVDVKKNVI ITISSDKGLC
     GGINSTSVKT SRNIHKLNSG PEKENKYVIL GEKAKAQLVR DSKKDIELII TELQKNPLNY
     TQVSVVADDI LKNVEFDALR IVFNKFQSVV SFVPTMSTVL SPEVVERESE SGGKLGDLDS
     YEIEGAESKS EVLQNLTEFQ FSSVLFNAVL ENACSEQGAR MSAMDSSSRN AGEMLDRLTL
     TYNRTRQASI TTELIEIISG ASALEG