ATPH_WHEAT
ID ATPH_WHEAT Reviewed; 81 AA.
AC P69448; P00843; Q33180; Q9XPT1;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=ATP synthase subunit c, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01396};
DE AltName: Full=ATP synthase F(0) sector subunit c {ECO:0000255|HAMAP-Rule:MF_01396};
DE AltName: Full=ATPase subunit III {ECO:0000255|HAMAP-Rule:MF_01396};
DE AltName: Full=F-type ATPase subunit c {ECO:0000255|HAMAP-Rule:MF_01396};
DE Short=F-ATPase subunit c {ECO:0000255|HAMAP-Rule:MF_01396};
DE AltName: Full=Lipid-binding protein {ECO:0000255|HAMAP-Rule:MF_01396};
GN Name=atpH {ECO:0000255|HAMAP-Rule:MF_01396};
OS Triticum aestivum (Wheat).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-40.
RX PubMed=16593250; DOI=10.1073/pnas.79.22.6903;
RA Howe C.J., Auffret A.D., Doherty A., Bowman C.M., Dyer T.A., Gray J.C.;
RT "Location and nucleotide sequence of the gene for the proton-translocating
RT subunit of wheat chloroplast ATP synthase.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:6903-6907(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring;
RA Ogihara Y., Isono K., Kojima T., Endo A., Hanaoka M., Shiina T.,
RA Terachi T., Utsugi S., Murata M., Mori N., Takumi S., Ikeo K., Gojobori T.,
RA Murai R., Murai K., Matsuoka Y., Ohnishi Y., Tajiri H., Tsunewaki K.;
RT "Chinese spring wheat (Triticum aestivum L.) chloroplast genome: complete
RT sequence and contig clones.";
RL Plant Mol. Biol. Rep. 18:243-253(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 62-81.
RX PubMed=16453616; DOI=10.1002/j.1460-2075.1985.tb03790.x;
RA Bird C.R., Koller B., Auffret A.D., Huttly A.K., Howe C.J., Dyer T.A.,
RA Gray J.C.;
RT "The wheat chloroplast gene for CF-0 subunit I of ATP synthase contains a
RT large intron.";
RL EMBO J. 4:1381-1388(1985).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
RC STRAIN=cv. Chinese Spring;
RX PubMed=10659768; DOI=10.1139/g99-062;
RA Ohnishi Y., Tajiri H., Matsuoka Y., Tsunewaki K.;
RT "Molecular analysis of a 21.1-kb fragment of wheat chloroplast DNA bearing
RT RNA polymerase subunit (rpo) genes.";
RL Genome 42:1042-1049(1999).
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:0000255|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:0000255|HAMAP-Rule:MF_01396}.
CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core
CC - and F(0) - the membrane proton channel. F(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has four main
CC subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains
CC form an alternating ring which encloses part of the gamma chain. F(1)
CC is attached to F(0) by a central stalk formed by the gamma and epsilon
CC chains, while a peripheral stalk is formed by the delta, b and b'
CC chains. {ECO:0000255|HAMAP-Rule:MF_01396}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01396}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01396}.
CC -!- MISCELLANEOUS: In plastids the F-type ATPase is also known as
CC CF(1)CF(0).
CC -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000255|HAMAP-
CC Rule:MF_01396}.
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DR EMBL; J01458; AAA84724.1; -; Genomic_DNA.
DR EMBL; AB042240; BAB47029.1; -; Genomic_DNA.
DR EMBL; X02595; CAA26440.1; -; Genomic_DNA.
DR EMBL; AB027572; BAA78045.1; -; Genomic_DNA.
DR RefSeq; NP_114254.1; NC_002762.1.
DR PDB; 4MJN; X-ray; 6.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-81.
DR PDBsum; 4MJN; -.
DR AlphaFoldDB; P69448; -.
DR SMR; P69448; -.
DR STRING; 4565.EPlTAEP00000010006; -.
DR EnsemblPlants; TraesCS1D02G180800.1; TraesCS1D02G180800.1.cds1; TraesCS1D02G180800.
DR EnsemblPlants; TraesCS5B02G052700.1; TraesCS5B02G052700.1.cds1; TraesCS5B02G052700.
DR EnsemblPlants; TraesCS5D02G196700.1; TraesCS5D02G196700.1.cds1; TraesCS5D02G196700.
DR GeneID; 803095; -.
DR Gramene; TraesCS1D02G180800.1; TraesCS1D02G180800.1.cds1; TraesCS1D02G180800.
DR Gramene; TraesCS5B02G052700.1; TraesCS5B02G052700.1.cds1; TraesCS5B02G052700.
DR Gramene; TraesCS5D02G196700.1; TraesCS5D02G196700.1.cds1; TraesCS5D02G196700.
DR KEGG; taes:803095; -.
DR eggNOG; KOG0232; Eukaryota.
DR HOGENOM; CLU_148047_2_0_1; -.
DR OMA; NIATVGY; -.
DR Proteomes; UP000019116; Chloroplast.
DR ExpressionAtlas; P69448; baseline.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
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:proton motive force-driven ATP synthesis; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; CF(0); Chloroplast; Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Lipid-binding; Membrane; Plastid;
KW Reference proteome; Thylakoid; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..81
FT /note="ATP synthase subunit c, chloroplastic"
FT /id="PRO_0000112207"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01396"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01396"
FT SITE 61
FT /note="Reversibly protonated during proton transport"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01396"
SQ SEQUENCE 81 AA; 7974 MW; 75F8DBD4F23A896D CRC64;
MNPLIAAASV IAAGLAVGLA SIGPGVGQGT AAGQAVEGIA RQPEAEGKIR GTLLLSLAFM
EALTIYGLVV ALALLFANPF V
