ID A0A7J8E6C1_ROUAE Unreviewed; 71 AA.
AC A0A7J8E6C1;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 17.
DE RecName: Full=ATP synthase F(0) complex subunit e, mitochondrial {ECO:0000256|ARBA:ARBA00074682, ECO:0000256|RuleBase:RU367005};
GN ORFNames=HJG63_001207 {ECO:0000313|EMBL:KAF6430779.1};
OS Rousettus aegyptiacus (Egyptian fruit bat) (Pteropus aegyptiacus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yinpterochiroptera; Pteropodoidea;
OC Pteropodidae; Rousettinae; Rousettus.
OX NCBI_TaxID=9407 {ECO:0000313|EMBL:KAF6430779.1, ECO:0000313|Proteomes:UP000593571};
RN [1] {ECO:0000313|EMBL:KAF6430779.1, ECO:0000313|Proteomes:UP000593571}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRouAeg1 {ECO:0000313|EMBL:KAF6430779.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAF6430779.1};
RX PubMed=32699395;
RA Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P.,
RA Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L.,
RA Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M.,
RA Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N.,
RA Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M.,
RA Vernes S.C., Myers E.W., Teeling E.C.;
RT "Six reference-quality genomes reveal evolution of bat adaptations.";
RL Nature 583:578-584(2020).
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|ARBA:ARBA00057306, ECO:0000256|RuleBase:RU367005}.
CC -!- SUBUNIT: Component of the ATP synthase complex composed at least of
CC ATP5F1A/subunit alpha, ATP5F1B/subunit beta, ATP5MC1/subunit c
CC (homooctomer), MT-ATP6/subunit a, MT-ATP8/subunit 8, ATP5ME/subunit e,
CC ATP5MF/subunit f, ATP5MG/subunit g, ATP5MK/subunit k, ATP5MJ/subunit j,
CC ATP5F1C/subunit gamma, ATP5F1D/subunit delta, ATP5F1E/subunit epsilon,
CC ATP5PF/subunit F6, ATP5PB/subunit b, ATP5PD/subunit d, ATP5PO/subunit
CC OSCP. ATP synthase complex consists of a soluble F(1) head domain
CC (subunits alpha(3) and beta(3)) - the catalytic core - and a membrane
CC F(0) domain - the membrane proton channel (subunits c, a, 8, e, f, g, k
CC and j). These two domains are linked by a central stalk (subunits
CC gamma, delta, and epsilon) rotating inside the F1 region and a
CC stationary peripheral stalk (subunits F6, b, d, and OSCP).
CC {ECO:0000256|ARBA:ARBA00064647}.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF6430779.1}.
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DR EMBL; JACASE010000010; KAF6430779.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7J8E6C1; -.
DR KEGG; ray:107518025; -.
DR CTD; 521; -.
DR OrthoDB; 9982108at2759; -.
DR Proteomes; UP000593571; 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 PANTHER; PTHR12427; ATP SYNTHASE E CHAIN, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12427:SF1; ATP SYNTHASE SUBUNIT E, MITOCHONDRIAL; 1.
DR Pfam; PF05680; ATP-synt_E; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310,
KW ECO:0000256|RuleBase:RU367005};
KW CF(0) {ECO:0000256|ARBA:ARBA00022547, ECO:0000256|RuleBase:RU367005};
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000593571};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367005}.
FT COILED 36..67
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 71 AA; 8205 MW; 1369CF2D873C39E2 CRC64;
MVPPVQVSPL IKLGRYSALF LGVAYGAKRY SYLKPRAEEE RRVAAEEKKK QDELKRIERE
LAEARDDSIL K
//
