ID A0A0C7N2Z0_9SACH Unreviewed; 92 AA.
AC A0A0C7N2Z0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=ATP synthase subunit e, mitochondrial {ECO:0000256|ARBA:ARBA00021462, ECO:0000256|RuleBase:RU367005};
GN ORFNames=LALA0_S05e04126g {ECO:0000313|EMBL:CEP62370.1};
OS Lachancea lanzarotensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1245769 {ECO:0000313|EMBL:CEP62370.1, ECO:0000313|Proteomes:UP000054304};
RN [1] {ECO:0000313|EMBL:CEP62370.1, ECO:0000313|Proteomes:UP000054304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 12615 {ECO:0000313|EMBL:CEP62370.1,
RC ECO:0000313|Proteomes:UP000054304};
RA Neuveglise Cecile;
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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; LN736364; CEP62370.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C7N2Z0; -.
DR STRING; 1245769.A0A0C7N2Z0; -.
DR HOGENOM; CLU_159435_1_0_1; -.
DR OrthoDB; 2043243at2759; -.
DR Proteomes; UP000054304; Unassembled WGS sequence.
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:UP000054304};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367005}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..92
FT /note="ATP synthase subunit e, mitochondrial"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002195480"
SQ SEQUENCE 92 AA; 10123 MW; 6A151480FD5DEF27 CRC64;
MSALNVFRYS AVLLGVAVGL QTDLSLKSQA SKQQEEKAYA EKLQLIEQAK AEYAKLHAPK
SETKTSNQKV DLEDPNLDYA KVILGAVESL KQ
//