ATPG_CHLRE
ID ATPG_CHLRE Reviewed; 358 AA.
AC P12113; Q9S884;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=ATP synthase gamma chain, chloroplastic {ECO:0000303|PubMed:8543042};
DE AltName: Full=F-ATPase gamma subunit;
DE Flags: Precursor;
GN Name=ATPC {ECO:0000303|PubMed:8543042};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2904436; DOI=10.1016/s0021-9258(19)77639-x;
RA Yu L.M., Selman B.R.;
RT "cDNA sequence and predicted primary structure of the gamma subunit from
RT the ATP synthase from Chlamydomonas reinhardtii.";
RL J. Biol. Chem. 263:19342-19345(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8349573; DOI=10.1007/bf00762588;
RA Smart E.J., Selman B.R.;
RT "Complementation of a Chlamydomonas reinhardtii mutant defective in the
RT nuclear gene encoding the chloroplast coupling factor 1 (CF1) gamma-subunit
RT (atpC).";
RL J. Bioenerg. Biomembr. 25:275-284(1993).
RN [3]
RP PROTEIN SEQUENCE OF 36-62, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
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).
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 {ECO:0000269|PubMed:8543042}.
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. The gamma chain is believed to be important in
CC regulating ATPase activity and the flow of protons through the CF(0)
CC complex.
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:0000269|PubMed:8543042}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:8543042}; Peripheral membrane protein
CC {ECO:0000269|PubMed:8543042}.
CC -!- MISCELLANEOUS: In plastids the F-type ATPase is also known as
CC CF(1)CF(0). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ATPase gamma chain family. {ECO:0000305}.
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DR EMBL; J04219; AAA33080.1; -; mRNA.
DR EMBL; M73493; AAA33079.1; -; Genomic_DNA.
DR PIR; A32004; PWKMG.
DR RefSeq; XP_001696335.1; XM_001696283.1.
DR AlphaFoldDB; P12113; -.
DR SMR; P12113; -.
DR STRING; 3055.EDP08312; -.
DR PRIDE; P12113; -.
DR ProMEX; P12113; -.
DR EnsemblPlants; PNW81779; PNW81779; CHLRE_06g259900v5.
DR GeneID; 5722055; -.
DR Gramene; PNW81779; PNW81779; CHLRE_06g259900v5.
DR KEGG; cre:CHLRE_06g259900v5; -.
DR eggNOG; KOG1531; Eukaryota.
DR HOGENOM; CLU_050669_0_0_1; -.
DR OMA; CGGYNNF; -.
DR OrthoDB; 841252at2759; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR CDD; cd12151; F1-ATPase_gamma; 1.
DR HAMAP; MF_00815; ATP_synth_gamma_bact; 1.
DR InterPro; IPR035968; ATP_synth_F1_ATPase_gsu.
DR InterPro; IPR000131; ATP_synth_F1_gsu.
DR InterPro; IPR023632; ATP_synth_F1_gsu_CS.
DR PANTHER; PTHR11693; PTHR11693; 1.
DR Pfam; PF00231; ATP-synt; 1.
DR PRINTS; PR00126; ATPASEGAMMA.
DR SUPFAM; SSF52943; SSF52943; 1.
DR TIGRFAMs; TIGR01146; ATPsyn_F1gamma; 1.
DR PROSITE; PS00153; ATPASE_GAMMA; 1.
PE 1: Evidence at protein level;
KW ATP synthesis; CF(1); Chloroplast; Direct protein sequencing;
KW Disulfide bond; Hydrogen ion transport; Ion transport; Membrane; Plastid;
KW Thylakoid; Transit peptide; Transport.
FT TRANSIT 1..35
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:8543042"
FT CHAIN 36..358
FT /note="ATP synthase gamma chain, chloroplastic"
FT /id="PRO_0000002676"
FT ACT_SITE 123
FT /evidence="ECO:0000250"
FT DISULFID 233..239
FT /evidence="ECO:0000250"
SQ SEQUENCE 358 AA; 38761 MW; 3E6685F60D6880C0 CRC64;
MAAMLASKQG AFMGRSSFAP APKGVASRGS LQVVAGLKEV RDRIASVKNT QKITDAMKLV
AAAKVRRAQE AVVNGRPFSE NLVKVLYGVN QRVRQEDVDS PLCAVRPVKS VLLVVLTGDR
GLCGGYNNFI IKKTEARYRE LTAMGVKVNL VCVGRKGAQY FARRKQYNIV KSFSLGAAPS
TKEAQGIADE IFASFIAQES DKVELVFTKF ISLINSNPTI QTLLPMTPMG ELCDVDGKCV
DAADDEIFKL TTKGGEFAVE REKTTIETEA LDPSLIFEQE PAQILDALLP LYMSSCLLRS
LQEALASELA ARMNAMNNAS DNAKELKKGL TVQYNKQRQA KITQELAEIV GGAAATSG
