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Database: UniProt
Entry: A0A2G2XBV2_CAPBA
LinkDB: A0A2G2XBV2_CAPBA
Original site: A0A2G2XBV2_CAPBA 
ID   A0A2G2XBV2_CAPBA        Unreviewed;       670 AA.
AC   A0A2G2XBV2;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=ATP synthase subunit alpha, chloroplastic {ECO:0000313|EMBL:PHT54968.1};
GN   ORFNames=CQW23_03454 {ECO:0000313|EMBL:PHT54968.1};
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:PHT54968.1, ECO:0000313|Proteomes:UP000224567};
RN   [1] {ECO:0000313|EMBL:PHT54968.1, 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:PHT54968.1};
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   -!- FUNCTION: This protein is one of the chains of the nonenzymatic
CC       membrane component (F0) of mitochondrial ATPase.
CC       {ECO:0000256|ARBA:ARBA00002351}.
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}. Plastid membrane
CC       {ECO:0000256|ARBA:ARBA00037835}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00037835}.
CC   -!- SIMILARITY: Belongs to the ATPase C chain family.
CC       {ECO:0000256|ARBA:ARBA00006704}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS2 family.
CC       {ECO:0000256|ARBA:ARBA00006242}.
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:PHT54968.1}.
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DR   EMBL; MLFT02000002; PHT54968.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G2XBV2; -.
DR   STRING; 33114.A0A2G2XBV2; -.
DR   Proteomes; UP000224567; Chromosome 2.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR   GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
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   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   CDD; cd18113; ATP-synt_F1_alpha_C; 1.
DR   CDD; cd18116; ATP-synt_F1_alpha_N; 1.
DR   CDD; cd01132; F1-ATPase_alpha_CD; 1.
DR   CDD; cd01425; RPS2; 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; 1.20.20.10; F1F0 ATP synthase subunit C; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_01346; ATP_synth_alpha_bact; 1.
DR   HAMAP; MF_00291_B; Ribosomal_S2_B; 1.
DR   InterPro; IPR000793; ATP_synth_asu_C.
DR   InterPro; IPR038376; ATP_synth_asu_C_sf.
DR   InterPro; IPR038662; ATP_synth_F0_csu_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; IPR002379; ATPase_proteolipid_c-like_dom.
DR   InterPro; IPR035921; F/V-ATP_Csub_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001865; Ribosomal_uS2.
DR   InterPro; IPR005706; Ribosomal_uS2_bac/mit/plastid.
DR   InterPro; IPR023591; Ribosomal_uS2_flav_dom_sf.
DR   NCBIfam; TIGR00962; atpA; 1.
DR   NCBIfam; TIGR01011; rpsB_bact; 1.
DR   PANTHER; PTHR48082; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48082:SF2; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF00306; ATP-synt_ab_C; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   Pfam; PF00137; ATP-synt_C; 1.
DR   Pfam; PF00318; Ribosomal_S2; 1.
DR   PRINTS; PR00395; RIBOSOMALS2.
DR   SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR   SUPFAM; SSF81333; F1F0 ATP synthase subunit C; 1.
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; 1.
DR   SUPFAM; SSF52313; Ribosomal protein S2; 1.
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   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   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   Thylakoid {ECO:0000256|ARBA:ARBA00023078};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          180..210
FT                   /note="V-ATPase proteolipid subunit C-like"
FT                   /evidence="ECO:0000259|Pfam:PF00137"
FT   DOMAIN          214..259
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02874"
FT   DOMAIN          295..528
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT                   nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00006"
FT   DOMAIN          535..659
FT                   /note="ATP synthase alpha subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00306"
SQ   SEQUENCE   670 AA;  73303 MW;  C5F44F7D3A9A6C9C CRC64;
     MTRRYWNINL EEMMEAGVHS GHGTRKWNPK MAPYISAKCK GIHITNLTRT AHFLSEACDL
     VFNAASRGKQ FLIVGTKNKA VDSVEWAAIR ARCHYVNKKW LGGSATIAVR NPQTIPTGGQ
     NFFEYVLEFI RDVGALLPWK VIQLPHGELT APTNDINTTV GLALLTSVAY FYEGLTRKGL
     GLASIGPGVG QGTAVGQAVE GIARQPEAEG KIRGDGIARI HGLDEVMAGE LVEFEEGTIG
     IALNLESNNV GVVLMGDAKP IDGRGEISAS EFRLIESAAP GIISRRSVYE PLQTGLIAID
     SMIPIGRGQR ELIIGDRQTG KTAVATDTIL NQQGQNAGKT AVATDTILNQ QGQHVICVYV
     AIGQKASSVD QVVTTLQERG AMEYTIVVAE TADSPATLQY LAPYTGAALA EYFMYRERHT
     LIIYDDLSKQ AQAYRQMYLL LRRPLGREDY PGDVFYLHSR ILERAAKLSS SLGEGSMTAL
     PIVETQSGDV SAYIPTNVIS ITDGQIFLSA DLFNSGIRPA INVGISISRV GSTAQIKAMK
     QVAGKLKLEL AQFAELEAFA QFASDLDKAT QNQLARGQRL RELLKQSQSA PLTVAEQIMT
     FYTGTNGYLY SLEVGQVRKF LVEIRTYLKT NKPQFQEIIS STKKFTEEVE SLLKEAIQEQ
     MDRFILQVQA
//
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