ID A0A2G2WJI2_CAPBA Unreviewed; 715 AA.
AC A0A2G2WJI2;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=ATP synthase subunit alpha, chloroplastic {ECO:0000313|EMBL:PHT45329.1};
GN ORFNames=CQW23_14487 {ECO:0000313|EMBL:PHT45329.1};
OS Capsicum baccatum (Peruvian pepper).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX NCBI_TaxID=33114 {ECO:0000313|EMBL:PHT45329.1, ECO:0000313|Proteomes:UP000224567};
RN [1] {ECO:0000313|EMBL:PHT45329.1, ECO:0000313|Proteomes:UP000224567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. PBC81 {ECO:0000313|Proteomes:UP000224567};
RC TISSUE=Leaf {ECO:0000313|EMBL:PHT45329.1};
RX PubMed=29089032; DOI=10.1186/s13059-017-1341-9;
RA Kim S., Park J., Yeom S.I., Kim Y.M., Seo E., Kim K.T., Kim M.S., Lee J.M.,
RA Cheong K., Shin H.S., Kim S.B., Han K., Lee J., Park M., Lee H.A.,
RA Lee H.Y., Lee Y., Oh S., Lee J.H., Choi E., Choi E., Lee S.E., Jeon J.,
RA Kim H., Choi G., Song H., Lee J., Lee S.C., Kwon J.K., Lee H.Y., Koo N.,
RA Hong Y., Kim R.W., Kang W.H., Huh J.H., Kang B.C., Yang T.J., Lee Y.H.,
RA Bennetzen J.L., Choi D.;
RT "New reference genome sequences of hot pepper reveal the massive evolution
RT of plant disease-resistance genes by retroduplication.";
RL Genome Biol. 18:R210.1-R210.11(2017).
RN [2] {ECO:0000313|Proteomes:UP000224567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. PBC81 {ECO:0000313|Proteomes:UP000224567};
RA Kim S., Park J., Yeom S.-I., Kim Y.-M., Seo E., Kim K.-T., Kim M.-S.,
RA Lee J.M., Cheong K., Shin H.-S., Kim S.-B., Han K., Lee J., Park M.,
RA Lee H.-A., Lee H.-Y., Lee Y., Oh S., Lee J.H., Choi E., Choi E., Lee S.E.,
RA Jeon J., Kim H., Choi G., Song H., Lee J., Lee S.-C., Kwon J.-K.,
RA Lee H.-Y., Koo N., Hong Y., Kim R.W., Kang W.-H., Huh J.H., Kang B.-C.,
RA Yang T.-J., Lee Y.-H., Bennetzen J.L., Choi D.;
RT "Multiple reference genome sequences of hot pepper reveal the massive
RT evolution of plant disease resistance genes by retroduplication.";
RL J. Anim. Genet. bioRxivorg:115410-115410(2017).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. The alpha chain is a regulatory subunit.
CC {ECO:0000256|ARBA:ARBA00003784}.
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 three main
CC subunits: a, b and c. {ECO:0000256|ARBA:ARBA00011648}.
CC -!- SUBCELLULAR LOCATION: Plastid membrane {ECO:0000256|ARBA:ARBA00037835};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00037835}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|RuleBase:RU000339}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PHT45329.1}.
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DR EMBL; MLFT02000006; PHT45329.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G2WJI2; -.
DR STRING; 33114.A0A2G2WJI2; -.
DR Proteomes; UP000224567; Chromosome 6.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
DR GO; GO:0042170; C:plastid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR GO; GO:0009579; C:thylakoid; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR CDD; cd18113; ATP-synt_F1_alpha_C; 2.
DR CDD; cd18116; ATP-synt_F1_alpha_N; 1.
DR CDD; cd01132; F1-ATPase_alpha_CD; 2.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 3.40.50.12240; -; 1.
DR Gene3D; 1.20.150.20; ATP synthase alpha/beta chain, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_01346; ATP_synth_alpha_bact; 1.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR000793; ATP_synth_asu_C.
DR InterPro; IPR038376; ATP_synth_asu_C_sf.
DR InterPro; IPR033732; ATP_synth_F1_a_nt-bd_dom.
DR InterPro; IPR005294; ATP_synth_F1_asu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00962; atpA; 1.
DR PANTHER; PTHR48082:SF12; ATP SYNTHASE SUBUNIT ALPHA, CHLOROPLASTIC; 1.
DR PANTHER; PTHR48082; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR Pfam; PF00006; ATP-synt_ab; 2.
DR Pfam; PF00306; ATP-synt_ab_C; 2.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 2.
DR SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW CF(1) {ECO:0000256|ARBA:ARBA00023196};
KW Chloroplast {ECO:0000256|ARBA:ARBA00022528};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW ECO:0000256|RuleBase:RU000339};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU000339}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Plastid {ECO:0000256|ARBA:ARBA00022640};
KW Reference proteome {ECO:0000313|Proteomes:UP000224567};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000339}.
FT DOMAIN 29..93
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 120..320
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
FT DOMAIN 315..399
FT /note="ATP synthase alpha subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00306"
FT DOMAIN 381..573
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
FT DOMAIN 580..704
FT /note="ATP synthase alpha subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00306"
SQ SEQUENCE 715 AA; 78364 MW; 16AFFC8B0CDC2450 CRC64;
MVTIRADEIS NIICECIEQY NREVKIVNTG TVLQVGDAIA RIHGLDEVMA GELVEFEEGT
IGIALNLESN NVGVVLMGDG LLIQERSSVK EMGRIAQIPV SEAYLGRVVN ALAKPIDGRG
RGQRELIIGD RQTGKTAVAT DTILNQQGQN VICVYVAIGQ KASSVAQVVT TLQERGAMEY
TIVVAETADS PATLQYLAPY TGAALAEYFM YRERHTLIIY DDLSKQAQAY RQMSLLLRRP
PGREAYLGDV FYLHSRLLER DAKLSSSLGE GSMTALPIVE TQSGDVSAYI PTNVISITDG
QIFLSADLFN SGIRLAINVE LEAFAQFASN LNKATQNQLA RGQRLREFLK QSQLASLTVA
EQIMTIYTGT NGYLDSLEVG QTGKTAVATD TILNQQGQNV ICVYVAIGQK ASSVAQVVTT
LQERGAMEYT IVVAETADSP ATLQYLAPYT GAALAEYFMY RERHTLIIYD DLSKQAQAYR
QMSLLLRRPP GREAYPGDVF YLHSRLLERA AKLSSSLGEG SMTALPIVET QSGDVSAYIP
TNVISITDGQ IFLSADLFNS GIRPAINVGI SVSRVGSAAQ IKAMKQVAGK LKLELAQFAE
LEAFAQFASD LDKATQNQLA RGQRLRELLK QSQSAPLTVA EQIMTIYTGT NGYLDSLEVG
QVRKFLVELR TYLKTNKPQF QEIISSTKKF TEEAEALLKE AIQEQMDRFI LQEQA
//
