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ATP synthase subunit c, chloroplastic (Fragment)

 Q4FGE8_TYPLA            Unreviewed;        81 AA.
Q4FGE8;
30-AUG-2005, integrated into UniProtKB/TrEMBL.
30-AUG-2005, sequence version 1.
25-OCT-2017, entry version 79.
RecName: Full=ATP synthase subunit c, chloroplastic {ECO:0000256|RuleBase:RU004221};
Flags: Fragment;
Name=atpH {ECO:0000313|EMBL:AAZ03827.1};
Typha latifolia (Bulrush) (Broadleaf cattail).
Plastid; Chloroplast {ECO:0000313|EMBL:AAZ03827.1}.
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Typhaceae; Typha.
NCBI_TaxID=4733 {ECO:0000313|EMBL:AAZ03827.1};
[1] {ECO:0000313|EMBL:AAZ03827.1}
NUCLEOTIDE SEQUENCE.
PubMed=15944438; DOI=10.1093/molbev/msi191;
Leebens-Mack J., Raubeson L.A., Cui L., Kuehl J.V., Fourcade M.H.,
Chumley T.W., Boore J.L., Jansen R.K., dePamphilis C.W.;
"Identifying the basal angiosperm node in chloroplast genome
phylogenies: sampling one's way out of the Felsenstein zone.";
Mol. Biol. Evol. 22:1948-1963(2005).
[2] {ECO:0000313|EMBL:AAZ03827.1}
NUCLEOTIDE SEQUENCE.
Leebens-Mack J.H., Raubeson L.A., Cui L., Kuehl J.V., Fourcade M.H.,
Chumley T.W., Boore J.L., Jansen R.K., dePamphilis C.W.;
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000313|EMBL:ADA63686.1}
NUCLEOTIDE SEQUENCE.
PubMed=18048330; DOI=10.1073/pnas.0709121104;
Jansen R.K., Cai Z., Raubeson L.A., Daniell H., dePamphilis C.W.,
Leebens-Mack J., Muller K.F., Guisinger-Bellian M., Haberle R.C.,
Hansen A.K., Chumley T.W., Lee S.B., Peery R., McNeal J.R.,
Kuehl J.V., Boore J.L.;
"Analysis of 81 genes from 64 plastid genomes resolves relationships
in angiosperms and identifies genome-scale evolutionary patterns.";
Proc. Natl. Acad. Sci. U.S.A. 104:19369-19374(2007).
[4] {ECO:0000313|EMBL:ADA63686.1}
NUCLEOTIDE SEQUENCE.
PubMed=20091301; DOI=10.1007/s00239-009-9317-3;
Guisinger M.M., Chumley T.W., Kuehl J.V., Boore J.L., Jansen R.K.;
"Implications of the Plastid Genome Sequence of Typha (Typhaceae,
Poales) for Understanding Genome Evolution in Poaceae.";
J. Mol. Evol. 70:149-166(2010).
-!- 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|RuleBase:RU004221}.
-!- 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. {ECO:0000256|RuleBase:RU004221}.
-!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic
core - and F(0) - the membrane proton channel. F(1) has five
subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0)
has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha
and beta chains form an alternating ring which encloses part of
the gamma chain. F(1) is attached to F(0) by a central stalk
formed by the gamma and epsilon chains, while a peripheral stalk
is formed by the delta, b and b' chains.
{ECO:0000256|RuleBase:RU004221}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
{ECO:0000256|RuleBase:RU004221}; Multi-pass membrane protein
{ECO:0000256|RuleBase:RU004221}.
-!- SIMILARITY: Belongs to the ATPase C chain family.
{ECO:0000256|RuleBase:RU004221}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|RuleBase:RU004221}.
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EMBL; DQ069383; AAZ03827.1; -; Genomic_DNA.
EMBL; GU195652; ADA63686.1; -; Genomic_DNA.
RefSeq; YP_003433962.1; NC_013823.1.
SMR; Q4FGE8; -.
GeneID; 8774468; -.
GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
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|RuleBase:RU004221};
CF(0) {ECO:0000256|RuleBase:RU004221};
Chloroplast {ECO:0000256|RuleBase:RU004221,
ECO:0000313|EMBL:AAZ03827.1};
Hydrogen ion transport {ECO:0000256|RuleBase:RU004221};
Ion transport {ECO:0000256|RuleBase:RU004221};
Lipid-binding {ECO:0000256|RuleBase:RU004221};
Membrane {ECO:0000256|RuleBase:RU004221};
Plastid {ECO:0000256|RuleBase:RU004221, ECO:0000313|EMBL:AAZ03827.1};
Thylakoid {ECO:0000256|RuleBase:RU004221};
Transmembrane {ECO:0000256|RuleBase:RU004221};
Transmembrane helix {ECO:0000256|RuleBase:RU004221};
Transport {ECO:0000256|RuleBase:RU004221}.
TRANSMEM 57 77 Helical. {ECO:0000256|RuleBase:RU004221}.
DOMAIN 11 73 ATP-synt_C. {ECO:0000259|Pfam:PF00137}.
NON_TER 81 81 {ECO:0000313|EMBL:AAZ03827.1}.
SEQUENCE 81 AA; 7990 MW; D418DBC23EE09FA1 CRC64;
MNPLISAASV IAAGLAVGLA SIGPGVGQGT AAGQAVEGIA RQPEAEGKIR GTLLLSLAFM
EALTIYGLVV ALALLFANPF V


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