ID   A0A0K0M2W3_9ASTR        Unreviewed;        81 AA.
AC   A0A0K0M2W3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   12-AUG-2020, entry version 21.
DE   RecName: Full=ATP synthase F0 sector subunit C {ECO:0000256|ARBA:ARBA00019198};
DE   AltName: Full=ATP synthase subunit C, plastid {ECO:0000256|ARBA:ARBA00020939};
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   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 between
RT   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 presence
CC       of a proton or sodium gradient. F-type ATPases consist of two
CC       structural domains, F(1) containing the extramembraneous catalytic core
CC       and F(0) containing the membrane proton channel, linked together by a
CC       central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC       in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC       the central stalk subunits to proton translocation. {ECO:0000256|HAMAP-
CC       Rule:MF_01396}.
CC   -!- FUNCTION: Key component of the F(0) channel; it plays a direct role in
CC       translocation across the membrane. A homomeric c-ring of between 10-14
CC       subunits forms the central stalk rotor element with the F(1) delta and
CC       epsilon subunits. {ECO:0000256|HAMAP-Rule:MF_01396}.
CC   -!- FUNCTION: This protein is one of the chains of the nonenzymatic
CC       membrane component (F0) of mitochondrial ATPase.
CC       {ECO:0000256|ARBA:ARBA00002351}.
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: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01396};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01396}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the ATPase C chain family.
CC       {ECO:0000256|ARBA:ARBA00006704, ECO:0000256|HAMAP-Rule:MF_01396,
CC       ECO:0000256|RuleBase:RU004221}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       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: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|ARBA:ARBA00023310, ECO:0000256|HAMAP-
KW   Rule:MF_01396}; Cell membrane {ECO:0000256|HAMAP-Rule:MF_01396};
KW   CF(0) {ECO:0000256|ARBA:ARBA00022547, ECO:0000256|HAMAP-Rule:MF_01396};
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, ECO:0000256|HAMAP-
KW   Rule:MF_01396, ECO:0000256|RuleBase:RU004221};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW   Rule:MF_01396, ECO:0000256|RuleBase:RU004221};
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00023121, ECO:0000256|HAMAP-
KW   Rule:MF_01396, ECO:0000256|RuleBase:RU004221};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01396,
KW   ECO:0000256|RuleBase:RU004221}; Plastid {ECO:0000313|EMBL:AJE74738.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_01396, ECO:0000256|RuleBase:RU004221};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_01396, ECO:0000256|RuleBase:RU004221};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01396,
KW   ECO:0000256|RuleBase:RU004221}.
FT   TRANSMEM        57..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01396,
FT                   ECO:0000256|RuleBase:RU004221"
FT   DOMAIN          11..73
FT                   /note="ATP-synt_C"
FT                   /evidence="ECO:0000259|Pfam:PF00137"
FT   SITE            61
FT                   /note="Reversibly protonated during proton transport"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01396"
SQ   SEQUENCE   81 AA;  7990 MW;  D418DBC23EE09FA1 CRC64;
     MNPLISAASV IAAGLAVGLA SIGPGVGQGT AAGQAVEGIA RQPEAEGKIR GTLLLSLAFM
     EALTIYGLVV ALALLFANPF V
//