ATPG_KLULA
ID ATPG_KLULA Reviewed; 289 AA.
AC P49377;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=ATP synthase subunit gamma, mitochondrial;
DE AltName: Full=F-ATPase gamma subunit;
DE Flags: Precursor;
GN Name=ATP3; Synonyms=MGI5; OrderedLocusNames=KLLA0B06886g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF THR-275.
RC STRAIN=ATCC 76492 / CBS 2359/152 / CLIB 210;
RX PubMed=7621839; DOI=10.1002/j.1460-2075.1995.tb07331.x;
RA Chen X.J., Clark-Walker G.D.;
RT "Specific mutations in alpha- and gamma-subunits of F1-ATPase affect
RT mitochondrial genome integrity in the petite-negative yeast Kluyveromyces
RT lactis.";
RL EMBO J. 14:3277-3286(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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:0000305}; Peripheral membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ATPase gamma chain family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X81711; CAA57355.1; -; Genomic_DNA.
DR EMBL; CR382122; CAH02232.1; -; Genomic_DNA.
DR PIR; S56153; S56153.
DR RefSeq; XP_451839.1; XM_451839.1.
DR AlphaFoldDB; P49377; -.
DR SMR; P49377; -.
DR STRING; 28985.XP_451839.1; -.
DR PRIDE; P49377; -.
DR EnsemblFungi; CAH02232; CAH02232; KLLA0_B06886g.
DR GeneID; 2897171; -.
DR KEGG; kla:KLLA0_B06886g; -.
DR eggNOG; KOG1531; Eukaryota.
DR HOGENOM; CLU_050669_4_1_1; -.
DR InParanoid; P49377; -.
DR OMA; MQITSAM; -.
DR Proteomes; UP000000598; Chromosome B.
DR GO; GO:0005756; C:mitochondrial proton-transporting ATP synthase, central stalk; IEA:EnsemblFungi.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:EnsemblFungi.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:EnsemblFungi.
DR CDD; cd12151; F1-ATPase_gamma; 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); Hydrogen ion transport; Ion transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transit peptide; Transport.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..289
FT /note="ATP synthase subunit gamma, mitochondrial"
FT /id="PRO_0000002689"
FT MUTAGEN 275
FT /note="T->A: In MGI5-1; converts K.lactis into a petite-
FT positive form."
FT /evidence="ECO:0000269|PubMed:7621839"
SQ SEQUENCE 289 AA; 31591 MW; 947A425FCA4DB864 CRC64;
MFVRNTASVV RGTSRNYATL REIETRLKSI KNIEKITKTM KIVASTRLSK AERAKNSAKE
YALADAAFYK NAETVPLEDA EKKDLIIAIT SDKGLCGSIH SQLAKAVRLQ LKQTPNADVV
AIGDKVKGQL LRTNSDNLKF AFNGVGKEAP TFEETSLIAN KILEGGASNY KKVSIFWNDP
ISSLSFEPSN KPVFNAAAIE QSPSFSKFEI DADNNVSQDL FEFTLSNEIL AAMAEGYAAE
VSARRNAMDN ASKNAGDMIN SYSILYNRTR QAVITNELVD IITGASSLD
