ATPH_SPIOL
ID ATPH_SPIOL Reviewed; 81 AA.
AC P69447; 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 90.
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 Spinacia oleracea (Spinach).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP PROTEIN SEQUENCE, AND FORMYLATION AT MET-1.
RA Sebald W., Wachter E.;
RT "Amino acid sequence of the proteolipid subunit of the ATP synthase from
RT spinach chloroplasts.";
RL FEBS Lett. 122:307-311(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Alt J., Winter P., Sebald W., Moser J.G., Schedel R., Westhoff P.,
RA Herrmann R.G.;
RT "Localization and nucleotide sequence of the gene for the ATP synthase
RT proteolipid subunit on the spinach plastid chromosome.";
RL Curr. Genet. 7:129-138(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Hennig J., Herrmann R.G.;
RT "Chloroplast ATP synthase of spinach contains nine nonidentical subunit
RT species, six of which are encoded by plastid chromosomes in two operons in
RT a phylogenetically conserved arrangement.";
RL Mol. Gen. Genet. 203:117-128(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2443718; DOI=10.1016/0022-2836(87)90690-5;
RA Hudson G.S., Mason J.G., Holton T.A., Koller B., Cox G.B., Whitfeld P.R.,
RA Bottomley W.;
RT "A gene cluster in the spinach and pea chloroplast genomes encoding one CF1
RT and three CF0 subunits of the H+-ATP synthase complex and the ribosomal
RT protein S2.";
RL J. Mol. Biol. 196:283-298(1987).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Geant d'hiver, and cv. Monatol;
RX PubMed=11292076; DOI=10.1023/a:1006478403810;
RA Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., Herrmann R.G.,
RA Mache R.;
RT "The plastid chromosome of spinach (Spinacia oleracea): complete nucleotide
RT sequence and gene organization.";
RL Plant Mol. Biol. 45:307-315(2001).
RN [6]
RP SUBUNIT, PRELIMINARY CRYSTALLIZATION, AND PIGMENT COMPOSITION.
RX PubMed=18515064; DOI=10.1016/j.bbabio.2008.05.009;
RA Varco-Merth B., Fromme R., Wang M., Fromme P.;
RT "Crystallization of the c14-rotor of the chloroplast ATP synthase reveals
RT that it contains pigments.";
RL Biochim. Biophys. Acta 1777:605-612(2008).
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.
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 14 subunits
CC forms the central stalk rotor element with the F(1) delta and epsilon
CC subunits.
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(14). The alpha and beta chains form
CC an alternating ring which encloses part of the gamma chain. F(1) is
CC 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:0000269|PubMed:18515064}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-
CC pass membrane protein.
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; X03775; CAA27402.1; -; Genomic_DNA.
DR EMBL; AJ400848; CAB88712.1; -; Genomic_DNA.
DR PIR; S14423; LWSPA.
DR RefSeq; NP_054919.1; NC_002202.1.
DR PDB; 2W5J; X-ray; 3.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/V=2-79.
DR PDB; 6FKF; EM; 3.10 A; G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-81.
DR PDB; 6FKH; EM; 4.20 A; G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-81.
DR PDB; 6FKI; EM; 4.30 A; G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-81.
DR PDB; 6TQJ; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-81.
DR PDB; 6VM1; EM; 7.90 A; M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z=1-81.
DR PDB; 6VM4; EM; 7.08 A; M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z=1-81.
DR PDB; 6VMB; EM; 5.23 A; M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z=1-81.
DR PDB; 6VMG; EM; 6.46 A; M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z=1-81.
DR PDB; 6VOF; EM; 4.51 A; M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z=1-81.
DR PDB; 6VOH; EM; 4.16 A; M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z=1-81.
DR PDB; 6VOJ; EM; 4.34 A; M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z=1-81.
DR PDB; 6VOL; EM; 4.06 A; M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z=1-81.
DR PDB; 6VON; EM; 3.35 A; M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z=1-81.
DR PDBsum; 2W5J; -.
DR PDBsum; 6FKF; -.
DR PDBsum; 6FKH; -.
DR PDBsum; 6FKI; -.
DR PDBsum; 6TQJ; -.
DR PDBsum; 6VM1; -.
DR PDBsum; 6VM4; -.
DR PDBsum; 6VMB; -.
DR PDBsum; 6VMG; -.
DR PDBsum; 6VOF; -.
DR PDBsum; 6VOH; -.
DR PDBsum; 6VOJ; -.
DR PDBsum; 6VOL; -.
DR PDBsum; 6VON; -.
DR AlphaFoldDB; P69447; -.
DR SMR; P69447; -.
DR IntAct; P69447; 1.
DR STRING; 3562.P69447; -.
DR ChEMBL; CHEMBL2366567; -.
DR GeneID; 2715579; -.
DR KEGG; soe:2715579; -.
DR OrthoDB; 1582734at2759; -.
DR BRENDA; 7.1.2.2; 5812.
DR EvolutionaryTrace; P69447; -.
DR PRO; PR:P69447; -.
DR Proteomes; UP000054095; Chloroplast.
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 Formylation; Hydrogen ion transport; Ion transport; Lipid-binding;
KW Membrane; Plastid; Reference proteome; Thylakoid; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..81
FT /note="ATP synthase subunit c, chloroplastic"
FT /id="PRO_0000112205"
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"
FT MOD_RES 1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000269|Ref.1"
FT HELIX 2..19
FT /evidence="ECO:0007829|PDB:6TQJ"
FT HELIX 22..41
FT /evidence="ECO:0007829|PDB:6TQJ"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:6TQJ"
FT HELIX 46..76
FT /evidence="ECO:0007829|PDB:6TQJ"
SQ SEQUENCE 81 AA; 7974 MW; 75F8DBD4F23A896D CRC64;
MNPLIAAASV IAAGLAVGLA SIGPGVGQGT AAGQAVEGIA RQPEAEGKIR GTLLLSLAFM
EALTIYGLVV ALALLFANPF V
