ATPH_CHLRE
ID ATPH_CHLRE Reviewed; 82 AA.
AC Q37304; B7U1J3; Q9T2G4;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=ATP synthase subunit c, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01396, ECO:0000303|PubMed:8543042};
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, ECO:0000303|PubMed:8543042};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cw15;
RX PubMed=9362486; DOI=10.1093/emboj/16.22.6713;
RA Rolland N., Dorne A.-J., Amoroso G., Sueltemeyer D.F., Joyard J.,
RA Rochaix J.-D.;
RT "Disruption of the plastid ycf10 open reading frame affects uptake of
RT inorganic carbon in the chloroplast of Chlamydomonas.";
RL EMBO J. 16:6713-6726(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=19473533; DOI=10.1186/1471-2148-9-120;
RA Smith D.R., Lee R.W.;
RT "Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome:
RT addressing the mutational-hazard hypothesis.";
RL BMC Evol. Biol. 9:120-120(2009).
RN [3]
RP PROTEIN SEQUENCE OF 1-32, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP FORMYLATION AT MET-1.
RC STRAIN=cw15;
RX PubMed=8543042; DOI=10.1016/0014-5793(95)01332-6;
RA Fiedler H.R., Schmid R., Leu S., Shavit N., Strotmann H.;
RT "Isolation of CF0CF1 from Chlamydomonas reinhardtii cw15 and the N-terminal
RT amino acid sequences of the CF0CF1 subunits.";
RL FEBS Lett. 377:163-166(1995).
RN [4]
RP IDENTIFICATION, AND COMPLETE PLASTID GENOME.
RX PubMed=12417694; DOI=10.1105/tpc.006155;
RA Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W., Harris E.H.,
RA Stern D.B.;
RT "The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a
RT sea of repeats.";
RL Plant Cell 14:2659-2679(2002).
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, ECO:0000269|PubMed:8543042}.
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, ECO:0000269|PubMed:8543042}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:8543042}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- MISCELLANEOUS: In plastids the F-type ATPase is also known as
CC CF(1)CF(0).
CC -!- MISCELLANEOUS: Dicyclohexylcarbodiimide (DCDD) inhibits ATPase.
CC -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000255|HAMAP-
CC Rule:MF_01396}.
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DR EMBL; X90559; CAA62149.1; -; Genomic_DNA.
DR EMBL; FJ423446; ACJ50140.1; -; Genomic_DNA.
DR EMBL; BK000554; DAA00954.1; -; Genomic_DNA.
DR PIR; S58349; S58349.
DR RefSeq; NP_958409.1; NC_005353.1.
DR AlphaFoldDB; Q37304; -.
DR SMR; Q37304; -.
DR STRING; 3055.DAA00954; -.
DR PaxDb; Q37304; -.
DR GeneID; 2717044; -.
DR KEGG; cre:ChreCp053; -.
DR eggNOG; KOG0232; Eukaryota.
DR HOGENOM; CLU_148047_2_0_1; -.
DR InParanoid; Q37304; -.
DR OrthoDB; 1582734at2759; -.
DR Proteomes; UP000006906; 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 ATP synthesis; CF(0); Chloroplast; Direct protein sequencing; Formylation;
KW Hydrogen ion transport; Ion transport; Lipid-binding; Membrane; Plastid;
KW Reference proteome; Thylakoid; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..82
FT /note="ATP synthase subunit c, chloroplastic"
FT /id="PRO_0000112184"
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|PubMed:8543042"
FT VARIANT 8
FT /note="T -> A (in strain: CC-503)"
SQ SEQUENCE 82 AA; 8093 MW; BFDC3BAF43E96A45 CRC64;
MNPIVAATSV VSAGLAVGLA AIGPGMGQGT AAGYAVEGIA RQPEAEGKIR GALLLSFAFM
ESLTIYGLVV ALALLFANPF AG
