ID A0A342LHH7_EPIBA Unreviewed; 225 AA. AC A0A342LHH7; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 14-DEC-2022, entry version 13. DE RecName: Full=ATP synthase subunit a {ECO:0000256|ARBA:ARBA00021312, ECO:0000256|RuleBase:RU004450}; GN Name=ATP6 {ECO:0000313|EMBL:ANW37014.1}; OS Episyrphus balteatus (Marmalade hoverfly) (Syrphus balteaus). OG Mitochondrion {ECO:0000313|EMBL:ANW37014.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Syrphoidea; OC Syrphidae; Syrphinae; Syrphini; Episyrphus. OX NCBI_TaxID=286459 {ECO:0000313|EMBL:ANW37014.1}; RN [1] {ECO:0000313|EMBL:ANW37014.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=28276531; DOI=10.1038/srep44300; RA Pu D.Q., Liu H.L., Gong Y.Y., Ji P.C., Li Y.J., Mou F.S., Wei S.J.; RT "Mitochondrial genomes of the hoverflies Episyrphus balteatus and Eupeodes RT corollae (Diptera: Syrphidae), with a phylogenetic analysis of RT Muscomorpha."; RL Sci. Rep. 7:44300-44300(2017). 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 F(0) CC - containing the membrane proton channel, linked together by a central CC stalk and a peripheral stalk. During catalysis, ATP synthesis in the CC catalytic domain of F(1) is coupled via a rotary mechanism of the CC central stalk subunits to proton translocation. Key component of the CC proton channel; it may play a direct role in the translocation of CC protons across the membrane. {ECO:0000256|ARBA:ARBA00002070}. 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. {ECO:0000256|ARBA:ARBA00011648}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion CC inner membrane {ECO:0000256|RuleBase:RU004450}; Multi-pass membrane CC protein {ECO:0000256|RuleBase:RU004450}. CC -!- SIMILARITY: Belongs to the ATPase A chain family. CC {ECO:0000256|ARBA:ARBA00006810}. 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; KU351241; ANW37014.1; -; Genomic_DNA. DR AlphaFoldDB; A0A342LHH7; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); 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 Gene3D; 1.20.120.220; -; 1. DR InterPro; IPR000568; ATP_synth_F0_asu. DR InterPro; IPR023011; ATP_synth_F0_asu_AS. DR InterPro; IPR045083; ATP_synth_F0_asu_bact/mt. DR InterPro; IPR035908; F0_ATP_A_sf. DR PANTHER; PTHR11410; ATP SYNTHASE SUBUNIT A; 1. DR Pfam; PF00119; ATP-synt_A; 1. DR PRINTS; PR00123; ATPASEA. DR SUPFAM; SSF81336; F1F0 ATP synthase subunit A; 1. DR TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1. DR PROSITE; PS00449; ATPASE_A; 1. PE 3: Inferred from homology; KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310}; KW CF(0) {ECO:0000256|ARBA:ARBA00022547}; KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Mitochondrion {ECO:0000313|EMBL:ANW37014.1}; KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}. FT TRANSMEM 20..39 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 72..94 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 100..120 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" SQ SEQUENCE 225 AA; 25252 MW; FC83092735241A06 CRC64; MMTNLFSVFD PSSSILSLSL NWLSTFIGLL MIPSMYWFMP SRYHIIWNNI LTTLHKEFTV LLGNPNQKGM TLIFVSLFSL ILFNNFMGLF PYIFTSTSHL TLTLMLALPL WLAFMIYGWL NHTQHMFAHL VPQGTPGVLM PFMVCIETIS NVIRPGTLAV RLTANMIAGH LLMTLLGNTG PSLSSMIIIV LLIVQMLLLI LESAVAIIQS YVFAVLSTLY SSEVI //