ID   ATPH_CERDE              Reviewed;          81 AA.
AC   A8SE66;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 50.
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   Ceratophyllum demersum (Rigid hornwort) (Coontail).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ceratophyllales; Ceratophyllaceae;
OC   Ceratophyllum.
OX   NCBI_TaxID=4428;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18048334; DOI=10.1073/pnas.0708072104;
RA   Moore M.J., Bell C.D., Soltis P.S., Soltis D.E.;
RT   "Using plastid genome-scale data to resolve enigmatic relationships among
RT   basal angiosperms.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:19363-19368(2007).
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; EF614270; ABQ81437.1; -; Genomic_DNA.
DR   RefSeq; YP_001542434.1; NC_009962.1.
DR   AlphaFoldDB; A8SE66; -.
DR   SMR; A8SE66; -.
DR   GeneID; 5729391; -.
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); 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   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; CF(0); Chloroplast; Hydrogen ion transport; Ion transport;
KW   Lipid-binding; Membrane; Plastid; Thylakoid; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..81
FT                   /note="ATP synthase subunit c, chloroplastic"
FT                   /id="PRO_0000362895"
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;  8006 MW;  D418CD0EE4F6537B CRC64;
     MNPLISSASV IAAGLAVGLA SIGPGVGQGT AAGQAVEGIA RQPEAEGKIR GTLLLSLAFM
     EALTIYGLVV ALALLFANPF V