ATPG_SPIOL
ID ATPG_SPIOL Reviewed; 364 AA.
AC P05435;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 2.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=ATP synthase gamma chain, chloroplastic;
DE AltName: Full=F-ATPase gamma subunit;
DE Flags: Precursor;
GN Name=ATPC;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Leaf;
RX PubMed=2151716; DOI=10.1007/bf00019397;
RA Mason J.G., Whitfeld P.R.;
RT "The gamma-subunit of spinach chloroplast ATP synthase: isolation and
RT characterisation of cDNA and genomic clones.";
RL Plant Mol. Biol. 14:1007-1018(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Monatol; TISSUE=Seedling;
RA Oelmueller R.;
RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 36-364, AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=cv. Nobel;
RX PubMed=2896606; DOI=10.1016/0014-5793(88)80421-6;
RA Miki J., Maeda M., Mukohata Y., Futai M.;
RT "The gamma-subunit of ATP synthase from spinach chloroplasts. Primary
RT structure deduced from the cloned cDNA sequence.";
RL FEBS Lett. 232:221-226(1988).
RN [4]
RP PROTEIN SEQUENCE OF 42-51; 112-128 AND 273-282.
RX PubMed=8664275; DOI=10.1021/bi952913p;
RA Hightower K.E., McCarty R.E.;
RT "Proteolytic cleavage within a regulatory region of the gamma subunit of
RT chloroplast coupling factor 1.";
RL Biochemistry 35:4846-4851(1996).
RN [5]
RP DISULFIDE BOND, AND ACTIVE SITE.
RX PubMed=6233281; DOI=10.1016/s0021-9258(17)39869-1;
RA Moroney J.V., Fullmer C.S., McCarty R.E.;
RT "Characterization of the cysteinyl-containing peptides of the gamma subunit
RT of coupling factor 1.";
RL J. Biol. Chem. 259:7281-7285(1984).
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, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main
CC subunits: a, b, b' and c (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane;
CC Peripheral membrane protein.
CC -!- PTM: Disulfide bond; Cys-240 and Cys-246 are known to form a disulfide
CC bridge in the dark which gives rise to an inactive enzyme. Activation
CC can be brought about by a ferredoxin-dependent reduction of the
CC disulfide bond in the light.
CC -!- MISCELLANEOUS: Alkylation of Cys-130 results in the inactivation of ATP
CC synthesis.
CC -!- SIMILARITY: Belongs to the ATPase gamma chain family. {ECO:0000305}.
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DR EMBL; Y00758; CAA68727.1; -; mRNA.
DR EMBL; X76131; CAA53734.1; -; Genomic_DNA.
DR EMBL; X17257; CAA35158.1; -; Genomic_DNA.
DR PIR; S10163; PWSPG.
DR PDB; 6FKF; EM; 3.10 A; g=1-364.
DR PDB; 6FKH; EM; 4.20 A; g=1-364.
DR PDB; 6FKI; EM; 4.30 A; g=1-364.
DR PDB; 6VM1; EM; 7.90 A; g=1-364.
DR PDB; 6VM4; EM; 7.08 A; g=1-364.
DR PDB; 6VMB; EM; 5.23 A; g=1-364.
DR PDB; 6VMD; EM; 4.53 A; g=1-364.
DR PDB; 6VMG; EM; 6.46 A; g=1-364.
DR PDB; 6VOF; EM; 4.51 A; g=1-364.
DR PDB; 6VOG; EM; 4.35 A; g=1-364.
DR PDB; 6VOH; EM; 4.16 A; g=1-364.
DR PDB; 6VOI; EM; 4.03 A; g=1-364.
DR PDB; 6VOJ; EM; 4.34 A; g=1-364.
DR PDB; 6VOK; EM; 3.85 A; g=1-364.
DR PDB; 6VOL; EM; 4.06 A; g=1-364.
DR PDB; 6VOM; EM; 3.60 A; g=1-364.
DR PDB; 6VON; EM; 3.35 A; g=1-364.
DR PDB; 6VOO; EM; 3.05 A; g=1-364.
DR PDBsum; 6FKF; -.
DR PDBsum; 6FKH; -.
DR PDBsum; 6FKI; -.
DR PDBsum; 6VM1; -.
DR PDBsum; 6VM4; -.
DR PDBsum; 6VMB; -.
DR PDBsum; 6VMD; -.
DR PDBsum; 6VMG; -.
DR PDBsum; 6VOF; -.
DR PDBsum; 6VOG; -.
DR PDBsum; 6VOH; -.
DR PDBsum; 6VOI; -.
DR PDBsum; 6VOJ; -.
DR PDBsum; 6VOK; -.
DR PDBsum; 6VOL; -.
DR PDBsum; 6VOM; -.
DR PDBsum; 6VON; -.
DR PDBsum; 6VOO; -.
DR AlphaFoldDB; P05435; -.
DR SMR; P05435; -.
DR IntAct; P05435; 1.
DR ChEMBL; CHEMBL2366567; -.
DR PRIDE; P05435; -.
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 3D-structure; 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..41
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:8664275"
FT CHAIN 42..364
FT /note="ATP synthase gamma chain, chloroplastic"
FT /id="PRO_0000002680"
FT REGION 17..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 130
FT /evidence="ECO:0000269|PubMed:6233281"
FT DISULFID 240..246
FT /note="In inhibited form"
FT /evidence="ECO:0000269|PubMed:2896606,
FT ECO:0000269|PubMed:6233281"
FT HELIX 44..100
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 116..123
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 133..150
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 162..170
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 188..203
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 251..259
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 261..272
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 288..362
FT /evidence="ECO:0007829|PDB:6FKF"
SQ SEQUENCE 364 AA; 40074 MW; 94F0FA9B444B3EEA CRC64;
MACSLSFSSS VSTFHLPTTT QSTQAPPNNA TTLPTTNPIQ CANLRELRDR IGSVKNTQKI
TEAMKLVAAA KVRRAQEAVV NGRPFSETLV EVLYNMNEQL QTEDVDVPLT KIRTVKKVAL
MVVTGDRGLC GGFNNMLLKK AESRIAELKK LGVDYTIISI GKKGNTYFIR RPEIPVDRYF
DGTNLPTAKE AQAIADDVFS LFVSEEVDKV EMLYTKFVSL VKSDPVIHTL LPLSPKGEIC
DINGKCVDAA EDELFRLTTK EGKLTVERDM IKTETPAFSP ILEFEQDPAQ ILDALLPLYL
NSQILRALQE SLASELAARM TAMSNATDNA NELKKTLSIN YNRARQAKIT GEILEIVAGA
NACV
