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Entry: C5DHF7_LACTC
LinkDB: C5DHF7_LACTC
Original site: C5DHF7_LACTC 
ID   C5DHF7_LACTC            Unreviewed;        92 AA.
AC   C5DHF7;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=ATP synthase subunit e, mitochondrial {ECO:0000256|ARBA:ARBA00021462, ECO:0000256|RuleBase:RU367005};
GN   OrderedLocusNames=KLTH0E03982g {ECO:0000313|EMBL:CAR23218.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR23218.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR23218.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
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(0) domain. Minor subunit located with subunit a in the membrane.
CC       {ECO:0000256|RuleBase:RU367005}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel.
CC       {ECO:0000256|RuleBase:RU367005}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|RuleBase:RU367005}.
CC   -!- SIMILARITY: Belongs to the ATPase e subunit family.
CC       {ECO:0000256|ARBA:ARBA00007333, ECO:0000256|RuleBase:RU367005}.
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DR   EMBL; CU928169; CAR23218.1; -; Genomic_DNA.
DR   RefSeq; XP_002553655.1; XM_002553609.1.
DR   AlphaFoldDB; C5DHF7; -.
DR   STRING; 559295.C5DHF7; -.
DR   GeneID; 8291804; -.
DR   KEGG; lth:KLTH0E03982g; -.
DR   eggNOG; ENOG502SDS3; Eukaryota.
DR   HOGENOM; CLU_159435_1_0_1; -.
DR   InParanoid; C5DHF7; -.
DR   OMA; WARDHPS; -.
DR   OrthoDB; 2043243at2759; -.
DR   Proteomes; UP000002036; Chromosome E.
DR   GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-UniRule.
DR   GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
DR   InterPro; IPR008386; ATP_synth_F0_esu_mt.
DR   Pfam; PF05680; ATP-synt_E; 1.
PE   3: Inferred from homology;
KW   ATP synthesis {ECO:0000256|ARBA:ARBA00023310,
KW   ECO:0000256|RuleBase:RU367005};
KW   CF(0) {ECO:0000256|ARBA:ARBA00022547, ECO:0000256|RuleBase:RU367005};
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW   ECO:0000256|RuleBase:RU367005};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU367005}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW   ECO:0000256|RuleBase:RU367005};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792,
KW   ECO:0000256|RuleBase:RU367005};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002036};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367005}.
SQ   SEQUENCE   92 AA;  10146 MW;  8AC6A4EE27E43F7B CRC64;
     MSTVNVLRYS ALALGAIIGL KTDLSLKSEA AKSSQQKEYA EKLKLIEQAK AEYARLHAPK
     QVEKQADTKL DLEDPNLDYG KVILSAVESL KQ
//
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