ID A0A0D1YQ59_9EURO Unreviewed; 94 AA.
AC A0A0D1YQ59;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 18-JUN-2025, entry version 29.
DE RecName: Full=ATP synthase F(0) complex subunit e, mitochondrial {ECO:0000256|RuleBase:RU367005};
GN ORFNames=PV11_08948 {ECO:0000313|EMBL:KIV77123.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV77123.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV77123.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV77123.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Subunit e, of the mitochondrial membrane ATP synthase complex
CC (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the
CC presence of a proton gradient across the membrane which is generated by
CC electron transport complexes of the respiratory chain. ATP synthase
CC complex consist of a soluble F(1) head domain - the catalytic core
CC - and a membrane F(1) domain - the membrane proton channel. These two
CC domains are linked by a central stalk rotating inside the F(1) region
CC and a stationary peripheral stalk. During catalysis, ATP synthesis in
CC the catalytic domain of F(1) is coupled via a rotary mechanism of the
CC central stalk subunits to proton translocation. In vivo, can only
CC synthesize ATP although its ATP hydrolase activity can be activated
CC artificially in vitro. Part of the complex F(0) domain.
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. CF(1) and CF(0) have
CC multiple subunits. {ECO:0000256|RuleBase:RU367005}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|ARBA:ARBA00004273, 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; KN846954; KIV77123.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1YQ59; -.
DR STRING; 1016849.A0A0D1YQ59; -.
DR HOGENOM; CLU_159435_2_0_1; -.
DR OrthoDB; 2125027at2759; -.
DR Proteomes; UP000053599; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045259; C:proton-transporting ATP synthase complex; IEA:UniProtKB-KW.
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:UP000053599};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367005}.
SQ SEQUENCE 94 AA; 10288 MW; 9BBAE1120281DDC1 CRC64;
MSTSQGVNVL RWSALVAGIF YGFTHQRTIS ANTAAAHAHA EYQHKLDLIQ KAKAEYAKKK
LPPQSKTAGG DIITDPNDKN FDLEAYLTKV AAEN
//
