ATPG_TOBAC
ID ATPG_TOBAC Reviewed; 377 AA.
AC P29790;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=ATP synthase gamma chain, chloroplastic;
DE AltName: Full=F-ATPase gamma subunit;
DE Flags: Precursor;
GN Name=ATPC;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 56-60.
RC TISSUE=Leaf;
RX PubMed=1535803; DOI=10.1007/bf00027359;
RA Larsson K.H., Napier J.A., Gray J.C.;
RT "Import and processing of the precursor form of the gamma subunit of the
RT chloroplast ATP synthase from tobacco.";
RL Plant Mol. Biol. 19:343-349(1992).
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 {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATPase gamma chain family. {ECO:0000305}.
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DR EMBL; X63606; CAA45152.1; -; mRNA.
DR PIR; S22486; PWNTG.
DR RefSeq; NP_001312843.1; NM_001325914.1.
DR AlphaFoldDB; P29790; -.
DR SMR; P29790; -.
DR STRING; 4097.P29790; -.
DR PRIDE; P29790; -.
DR ProMEX; P29790; -.
DR GeneID; 107813955; -.
DR KEGG; nta:107813955; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); IBA:GO_Central.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
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 Reference proteome; Thylakoid; Transit peptide; Transport.
FT TRANSIT 1..55
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:1535803"
FT CHAIN 56..377
FT /note="ATP synthase gamma chain, chloroplastic"
FT /id="PRO_0000002681"
FT REGION 30..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 143
FT /evidence="ECO:0000250"
FT DISULFID 253..259
FT /evidence="ECO:0000250"
SQ SEQUENCE 377 AA; 41447 MW; 60A262F08013F3E0 CRC64;
MSCSNLTMLV SSKPSLSDSS ALSFRSSVSP FQLPNHNTSG PSNPSRSSSV TPVHCGLRDL
RDRIESVKNT QKITEAMKLV AAAKVRRAQE AVVGARPFSE TLVEVLYNIN EQLQTDDIDV
PLTKVRPVKK VALVVVTGDR GLCGGFNNYL IKKAEARIRD LKALGIDYTI ISVGKKGNSY
FIRRPYIPVD KFLEGSNLPT AKDAQAIADD VFSLFVSEEV DKVELLYTKF VSLVKSEPVI
HTLLPLSPKG EICDINGNCV DAANDEFFRL TTKEGKLTVE RDIIRTKTTD FSPILQFEQD
PVQILDALLP LYLNSQILRA LQESLASELA ARMSAMSSAT DNATELKKNL SRVYNRQRQA
KITGEILEIV AGADALV