ID A0A0K0M2W3_9ASTR Unreviewed; 81 AA. AC A0A0K0M2W3; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 27-SEP-2017, entry version 13. DE SubName: Full=ATP synthase CF0 C subunit {ECO:0000313|EMBL:AJE74738.1}; GN Name=atpE {ECO:0000256|HAMAP-Rule:MF_01396}; OS Hymenopappus tenuifolius. OG Plastid {ECO:0000313|EMBL:AJE74738.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; campanulids; Asterales; Asteraceae; OC Asteroideae; Heliantheae alliance; Bahieae; Hymenopappus. OX NCBI_TaxID=1552227 {ECO:0000313|EMBL:AJE74738.1}; RN [1] {ECO:0000313|EMBL:AJE74738.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=26191461; RA Kellar P.R., Ahrendsen D.L., Aust S.K., Jones A.R., Pires J.C.; RT "Biodiversity comparison among phylogenetic diversity metrics and RT between three North American prairies."; RL Appl Plant Sci 3:1400108-1400108(2015). CC -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the CC presence of a proton or sodium gradient. F-type ATPases consist of CC two structural domains, F(1) containing the extramembraneous CC catalytic core and F(0) containing the membrane proton channel, CC linked together by a central stalk and a peripheral stalk. During CC catalysis, ATP synthesis in the catalytic domain of F(1) is CC coupled via a rotary mechanism of the central stalk subunits to CC proton translocation. {ECO:0000256|HAMAP-Rule:MF_01396}. CC -!- FUNCTION: Key component of the F(0) channel; it plays a direct CC role in translocation across the membrane. A homomeric c-ring of CC between 10-14 subunits forms the central stalk rotor element with CC the F(1) delta and epsilon subunits. {ECO:0000256|HAMAP- CC Rule:MF_01396}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP- CC Rule:MF_01396}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01396}. CC -!- SIMILARITY: Belongs to the ATPase C chain family. CC {ECO:0000256|HAMAP-Rule:MF_01396, ECO:0000256|RuleBase:RU004221}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01396, CC ECO:0000256|RuleBase:RU004221}. 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; KP126891; AJE74738.1; -; Genomic_DNA. DR ProteinModelPortal; A0A0K0M2W3; -. DR SMR; A0A0K0M2W3; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009536; C:plastid; IEA:UniProtKB-KW. DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule. DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro. DR GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:UniProtKB-UniRule. DR Gene3D; 1.20.20.10; -; 1. DR HAMAP; MF_01396; ATP_synth_c_bact; 1. DR InterPro; IPR005953; ATP_synth_csu_bac/chlpt. DR InterPro; IPR000454; ATP_synth_F0_csu. DR InterPro; IPR020537; ATP_synth_F0_csu_DDCD_BS. DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom. DR PANTHER; PTHR10031; PTHR10031; 1. DR Pfam; PF00137; ATP-synt_C; 1. DR PRINTS; PR00124; ATPASEC. DR SUPFAM; SSF81333; SSF81333; 1. DR TIGRFAMs; TIGR01260; ATP_synt_c; 1. DR PROSITE; PS00605; ATPASE_C; 1. PE 3: Inferred from homology; KW ATP synthesis {ECO:0000256|HAMAP-Rule:MF_01396}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01396}; KW CF(0) {ECO:0000256|HAMAP-Rule:MF_01396}; KW Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01396, KW ECO:0000256|RuleBase:RU004221}; KW Ion transport {ECO:0000256|HAMAP-Rule:MF_01396, KW ECO:0000256|RuleBase:RU004221}; KW Lipid-binding {ECO:0000256|HAMAP-Rule:MF_01396, KW ECO:0000256|RuleBase:RU004221}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01396, KW ECO:0000256|RuleBase:RU004221}; KW Plastid {ECO:0000313|EMBL:AJE74738.1}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01396, KW ECO:0000256|RuleBase:RU004221}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01396, KW ECO:0000256|RuleBase:RU004221}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01396, KW ECO:0000256|RuleBase:RU004221}. FT TRANSMEM 57 77 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01396, ECO:0000256|RuleBase:RU004221}. FT DOMAIN 11 73 ATP-synt_C. {ECO:0000259|Pfam:PF00137}. FT SITE 61 61 Reversibly protonated during proton FT transport. {ECO:0000256|HAMAP-Rule: FT MF_01396}. SQ SEQUENCE 81 AA; 7990 MW; D418DBC23EE09FA1 CRC64; MNPLISAASV IAAGLAVGLA SIGPGVGQGT AAGQAVEGIA RQPEAEGKIR GTLLLSLAFM EALTIYGLVV ALALLFANPF V //