ATPH_PEA
ID ATPH_PEA Reviewed; 81 AA.
AC P08212;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 127.
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 Pisum sativum (Garden pea).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2129529; DOI=10.1016/0378-1119(90)90184-s;
RA Huttly A.K., Plant A.L., Phillips A.L., Auffret A.D., Gray J.C.;
RT "Nucleotide sequence and transcripts of the pea chloroplast gene encoding
RT CF0 subunit III of ATP synthase.";
RL Gene 90:227-233(1990).
RN [3]
RP PROTEIN SEQUENCE OF 1-32.
RX PubMed=16453667; DOI=10.1002/j.1460-2075.1986.tb04201.x;
RA Cozens A.L., Walker J.E., Phillips A.L., Huttly A.K., Gray J.C.;
RT "A sixth subunit of ATP synthase, an F(0) component, is encoded in the pea
RT chloroplast genome.";
RL EMBO J. 5:217-222(1986).
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; 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; X05917; CAA29350.1; -; Genomic_DNA.
DR EMBL; M57711; AAA84541.1; -; Genomic_DNA.
DR PIR; S14424; LWPMA.
DR RefSeq; YP_003587563.1; NC_014057.1.
DR PDB; 3V3C; X-ray; 3.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=3-81.
DR PDBsum; 3V3C; -.
DR AlphaFoldDB; P08212; -.
DR SMR; P08212; -.
DR EnsemblPlants; Psat1g099200.1; Psat1g099200.1.cds1; Psat1g099200.
DR EnsemblPlants; Psat7g033720.1; Psat7g033720.1.cds1; Psat7g033720.
DR GeneID; 9073115; -.
DR Gramene; Psat1g099200.1; Psat1g099200.1.cds1; Psat1g099200.
DR Gramene; Psat7g033720.1; Psat7g033720.1.cds1; Psat7g033720.
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 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 Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..81
FT /note="ATP synthase subunit c, chloroplastic"
FT /id="PRO_0000112201"
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 HELIX 4..20
FT /evidence="ECO:0007829|PDB:3V3C"
FT HELIX 22..41
FT /evidence="ECO:0007829|PDB:3V3C"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:3V3C"
FT HELIX 46..75
FT /evidence="ECO:0007829|PDB:3V3C"
SQ SEQUENCE 81 AA; 8032 MW; 75F8D929DDEA896D CRC64;
MNPLIAAASV IAAGLAVGLA SIGPGVGQGT AAGQAVEGIA RQPEAEDKIR GTLLLSLAFM
EALTIYGLVV ALALLFANPF V
