ID A0A2P1CLW1_9HEMI Unreviewed; 222 AA. AC A0A2P1CLW1; DT 23-MAY-2018, integrated into UniProtKB/TrEMBL. DT 23-MAY-2018, sequence version 1. DT 22-FEB-2023, entry version 11. DE RecName: Full=ATP synthase subunit a {ECO:0000256|ARBA:ARBA00021312, ECO:0000256|RuleBase:RU004450}; GN Name=ATP6 {ECO:0000313|EMBL:AVJ52312.1}; OS Chrysocoris stollii. OG Mitochondrion {ECO:0000313|EMBL:AVJ52312.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera; OC Pentatomomorpha; Pentatomoidea; Scutelleridae; Scutellerinae; Chrysocoris. OX NCBI_TaxID=1873032 {ECO:0000313|EMBL:AVJ52312.1}; RN [1] {ECO:0000313|EMBL:AVJ52312.1} RP NUCLEOTIDE SEQUENCE. RA Wu Y., Redei D., Eger J., Wang Y., Wu H., Carapezza A., Kment P., Cai B., RA Sun X., Guo P., Luo J., Xie Q.; RT "Phylogeny and the colourful history of jewel bugs (Insecta: Hemiptera: RT Scutelleridae)."; RL Cladistics 0:0-0(2018). 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; MF173668; AVJ52312.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2P1CLW1; -. 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 CDD; cd00310; ATP-synt_Fo_a_6; 1. DR Gene3D; 1.20.120.220; ATP synthase, F0 complex, subunit A; 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 PANTHER; PTHR11410:SF0; 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:AVJ52312.1}; 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..38 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 68..92 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 98..118 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 125..144 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 156..174 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 186..210 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" SQ SEQUENCE 222 AA; 25101 MW; CBE39F90F899A009 CRC64; MMTNLFSTFD PSTSMQLSMN WISTFIGLIM IPSTYWLLPN RMNILIFNTM NKLHEEFKLL LGLQNKGMTL MMITLFTFII FNNAMGLLPY VFTSSSHLVF TMTLALPLWL SIMIFGWINN TNHMFTHLVP TGTPAVLMPF MVLIETISNL IRPGSLAVRL TANMIAGHLL MSLLGNNSIN VNNMLLPIIM IIQMILMMFE TAVAVIQAYV FSVLSTLYTS EV //