ID   A0A0K0M2W3_9ASTR        Unreviewed;        81 AA.
AC   A0A0K0M2W3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   08-MAY-2019, entry version 18.
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}.
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DR   EMBL; KP126891; AJE74738.1; -; Genomic_DNA.
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; IPR038662; ATP_synth_F0_csu_sf.
DR   InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR   InterPro; IPR035921; F/V-ATP_Csub_sf.
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
//