ATPH_SOLLC
ID ATPH_SOLLC Reviewed; 81 AA.
AC Q2MIB3;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 76.
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 Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. LA3023;
RX PubMed=16575560; DOI=10.1007/s00122-006-0254-x;
RA Daniell H., Lee S.-B., Grevich J., Saski C., Quesada-Vargas T., Guda C.,
RA Tomkins J., Jansen R.K.;
RT "Complete chloroplast genome sequences of Solanum bulbocastanum, Solanum
RT lycopersicum and comparative analyses with other Solanaceae genomes.";
RL Theor. Appl. Genet. 112:1503-1518(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. IPA-6;
RX PubMed=16830097; DOI=10.1007/s00239-005-0254-5;
RA Kahlau S., Aspinall S., Gray J.C., Bock R.;
RT "Sequence of the tomato chloroplast DNA and evolutionary comparison of
RT solanaceous plastid genomes.";
RL J. Mol. Evol. 63:194-207(2006).
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; DQ347959; ABC56287.1; -; Genomic_DNA.
DR EMBL; AM087200; CAJ32380.1; -; Genomic_DNA.
DR RefSeq; AP_004915.1; AC_000188.1.
DR RefSeq; YP_008563075.1; NC_007898.3.
DR AlphaFoldDB; Q2MIB3; -.
DR SMR; Q2MIB3; -.
DR STRING; 4081.Solyc09g059660.1.1; -.
DR PaxDb; Q2MIB3; -.
DR GeneID; 3950479; -.
DR KEGG; sly:3950479; -.
DR eggNOG; KOG0232; Eukaryota.
DR InParanoid; Q2MIB3; -.
DR OrthoDB; 1582734at2759; -.
DR Proteomes; UP000004994; 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 3: Inferred from homology;
KW ATP synthesis; CF(0); Chloroplast; Hydrogen ion transport; Ion transport;
KW Lipid-binding; Membrane; Plastid; Reference proteome; Thylakoid;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..81
FT /note="ATP synthase subunit c, chloroplastic"
FT /id="PRO_0000277325"
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; 7990 MW; D418DBC23EE09FA1 CRC64;
MNPLISAASV IAAGLAVGLA SIGPGVGQGT AAGQAVEGIA RQPEAEGKIR GTLLLSLAFM
EALTIYGLVV ALALLFANPF V
