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ATP synthase CF0 C chain (ATP synthase CF0 subunit III)

 H2F520_9ASPA            Unreviewed;        81 AA.
H2F520;
21-MAR-2012, integrated into UniProtKB/TrEMBL.
21-MAR-2012, sequence version 1.
25-OCT-2017, entry version 32.
SubName: Full=ATP synthase CF0 C chain {ECO:0000313|EMBL:AEX93753.1};
SubName: Full=ATP synthase CF0 subunit III {ECO:0000313|EMBL:AFB18447.1};
Name=atpH {ECO:0000313|EMBL:AEX93753.1};
Synonyms=atpE {ECO:0000256|HAMAP-Rule:MF_01396};
Hosta ventricosa (blue plantain lily).
Plastid {ECO:0000313|EMBL:AEX93753.1}.
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Asparagales; Asparagaceae;
Agavoideae; Hosta.
NCBI_TaxID=39527 {ECO:0000313|EMBL:AEX93753.1};
[1] {ECO:0000313|EMBL:AFB18447.1}
NUCLEOTIDE SEQUENCE.
Givnish T.J., Ames M., McNeal J.R., McKain M.J., Steele P.R.,
dePamphilis C.W., Graham S.W., Pires J.C., Stevenson D.W.,
Zomlefer W.B., Briggs B.G., Duvall M.R., Moore M.J., Heaney J.M.,
Soltis D.E., Soltis P.S., Thiele K., Leebens-Mack J.H.;
"Assembling the Tree of the Monocotyledons: Plastome Sequence
Phylogeny and Evolution of Poales.";
Ann. Mo. Bot. Gard. 97:584-616(2010).
[2] {ECO:0000313|EMBL:AEX93753.1}
NUCLEOTIDE SEQUENCE.
PubMed=22291168; DOI=10.3732/ajb.1100491;
Steele P.R., Hertweck K.L., Mayfield D., McKain M.R., Leebens-Mack J.,
Pires J.C.;
"Quality and quantity of data recovered from massively parallel
sequencing: Examples in Asparagales and Poaceae.";
Am. J. Bot. 99:330-348(2012).
[3] {ECO:0000313|EMBL:APO12209.1}
NUCLEOTIDE SEQUENCE.
PubMed=27793858;
McKain M.R., McNeal J.R., Kellar P.R., Eguiarte L.E., Pires J.C.,
Leebens-Mack J.;
"Timing of rapid diversification and convergent origins of active
pollination within Agavoideae (Asparagaceae).";
Am. J. Bot. 103:1717-1729(2016).
-!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the
presence of a proton or sodium gradient. F-type ATPases consist of
two structural domains, F(1) containing the extramembraneous
catalytic core and F(0) containing the membrane proton channel,
linked together by a central stalk and a peripheral stalk. During
catalysis, ATP synthesis in the catalytic domain of F(1) is
coupled via a rotary mechanism of the central stalk subunits to
proton translocation. {ECO:0000256|HAMAP-Rule:MF_01396}.
-!- FUNCTION: Key component of the F(0) channel; it plays a direct
role in translocation across the membrane. A homomeric c-ring of
between 10-14 subunits forms the central stalk rotor element with
the F(1) delta and epsilon subunits. {ECO:0000256|HAMAP-
Rule:MF_01396}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
Rule:MF_01396}; Multi-pass membrane protein {ECO:0000256|HAMAP-
Rule:MF_01396}.
-!- SIMILARITY: Belongs to the ATPase C chain family.
{ECO:0000256|HAMAP-Rule:MF_01396, ECO:0000256|RuleBase:RU004221}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01396,
ECO:0000256|RuleBase:RU004221}.
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EMBL; JQ273793; AEX93753.1; -; Genomic_DNA.
EMBL; HQ180590; AFB18447.1; -; Genomic_DNA.
EMBL; KX931460; APO12209.1; -; Genomic_DNA.
RefSeq; YP_009335151.1; NC_032706.1.
ProteinModelPortal; H2F520; -.
SMR; H2F520; -.
GeneID; 30766898; -.
GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:UniProtKB-UniRule.
Gene3D; 1.20.20.10; -; 1.
HAMAP; MF_01396; ATP_synth_c_bact; 1.
InterPro; IPR005953; ATP_synth_csu_bac/chlpt.
InterPro; IPR000454; ATP_synth_F0_csu.
InterPro; IPR020537; ATP_synth_F0_csu_DDCD_BS.
InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
InterPro; IPR035921; F1F0_ATP_C_sf.
PANTHER; PTHR10031; PTHR10031; 1.
Pfam; PF00137; ATP-synt_C; 1.
PRINTS; PR00124; ATPASEC.
SUPFAM; SSF81333; SSF81333; 1.
TIGRFAMs; TIGR01260; ATP_synt_c; 1.
PROSITE; PS00605; ATPASE_C; 1.
3: Inferred from homology;
ATP synthesis {ECO:0000256|HAMAP-Rule:MF_01396};
Cell membrane {ECO:0000256|HAMAP-Rule:MF_01396};
CF(0) {ECO:0000256|HAMAP-Rule:MF_01396};
Chloroplast {ECO:0000313|EMBL:AEX93753.1};
Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01396};
Ion transport {ECO:0000256|HAMAP-Rule:MF_01396};
Lipid-binding {ECO:0000256|HAMAP-Rule:MF_01396,
ECO:0000256|RuleBase:RU004221};
Membrane {ECO:0000256|HAMAP-Rule:MF_01396,
ECO:0000256|RuleBase:RU004221}; Plastid {ECO:0000313|EMBL:AEX93753.1};
Transmembrane {ECO:0000256|HAMAP-Rule:MF_01396,
ECO:0000256|RuleBase:RU004221};
Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01396,
ECO:0000256|RuleBase:RU004221};
Transport {ECO:0000256|HAMAP-Rule:MF_01396}.
TRANSMEM 57 77 Helical. {ECO:0000256|HAMAP-
Rule:MF_01396,
ECO:0000256|RuleBase:RU004221}.
DOMAIN 11 73 ATP-synt_C. {ECO:0000259|Pfam:PF00137}.
SITE 61 61 Reversibly protonated during proton
transport. {ECO:0000256|HAMAP-
Rule:MF_01396}.
NON_TER 81 81 {ECO:0000313|EMBL:AFB18447.1}.
SEQUENCE 81 AA; 7990 MW; D418DBC23EE09FA1 CRC64;
MNPLISAASV IAAGLAVGLA SIGPGVGQGT AAGQAVEGIA RQPEAEGKIR GTLLLSLAFM
EALTIYGLVV ALALLFANPF V


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