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Database: UniProt
Entry: Q4FGJ4_ACOAM
LinkDB: Q4FGJ4_ACOAM
Original site: Q4FGJ4_ACOAM 
ID   Q4FGJ4_ACOAM            Unreviewed;       506 AA.
AC   Q4FGJ4;
DT   30-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2005, sequence version 1.
DT   24-JAN-2024, entry version 81.
DE   RecName: Full=ATP synthase subunit alpha, chloroplastic {ECO:0000256|RuleBase:RU004286};
DE            EC=7.1.2.2 {ECO:0000256|RuleBase:RU004286};
DE   Flags: Fragment;
GN   Name=atpA {ECO:0000256|RuleBase:RU004286,
GN   ECO:0000313|EMBL:AAZ03781.1};
OS   Acorus americanus (Sweetflag) (Acorus calamus var. americanus).
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AAZ03781.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Acoraceae; Acorus.
OX   NCBI_TaxID=263995 {ECO:0000313|EMBL:AAZ03781.1};
RN   [1] {ECO:0000313|EMBL:AAZ03781.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15944438; DOI=10.1093/molbev/msi191;
RA   Leebens-Mack J., Raubeson L.A., Cui L., Kuehl J.V., Fourcade M.H.,
RA   Chumley T.W., Boore J.L., Jansen R.K., dePamphilis C.W.;
RT   "Identifying the basal angiosperm node in chloroplast genome phylogenies:
RT   sampling one's way out of the Felsenstein zone.";
RL   Mol. Biol. Evol. 22:1948-1963(2005).
RN   [2] {ECO:0000313|EMBL:AAZ03781.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Leebens-Mack J.H., Raubeson L.A., Cui L., Kuehl J.V., Fourcade M.H.,
RA   Chumley T.W., Boore J.L., Jansen R.K., dePamphilis C.W.;
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|RuleBase:RU004286}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC         Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC         Evidence={ECO:0000256|RuleBase:RU004286};
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. {ECO:0000256|RuleBase:RU004286}.
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}. Plastid,
CC       chloroplast thylakoid membrane {ECO:0000256|RuleBase:RU000341};
CC       Peripheral membrane protein {ECO:0000256|RuleBase:RU000341}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|RuleBase:RU000339}.
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DR   EMBL; DQ069337; AAZ03781.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4FGJ4; -.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
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   Gene3D; 2.40.30.20; -; 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; 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   PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 1.
DR   SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 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   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis {ECO:0000256|ARBA:ARBA00023310,
KW   ECO:0000256|RuleBase:RU004286};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004286};
KW   CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|RuleBase:RU004286};
KW   Chloroplast {ECO:0000256|RuleBase:RU000341, ECO:0000313|EMBL:AAZ03781.1};
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};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU004286};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004286};
KW   Plastid {ECO:0000256|RuleBase:RU004286, ECO:0000313|EMBL:AAZ03781.1};
KW   Thylakoid {ECO:0000256|RuleBase:RU000341};
KW   Translocase {ECO:0000256|RuleBase:RU004286};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000339}.
FT   DOMAIN          28..93
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02874"
FT   DOMAIN          150..365
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT                   nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00006"
FT   DOMAIN          372..496
FT                   /note="ATP synthase alpha subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00306"
FT   NON_TER         506
FT                   /evidence="ECO:0000313|EMBL:AAZ03781.1"
SQ   SEQUENCE   506 AA;  55252 MW;  DC9AFF0B36E786D8 CRC64;
     MATLRADEIS NIIRERIEQY TREVKVVNTG TVLQVGDGIA RIHGLDEVMA GELVEFEEGT
     IGIALNLESN NVGVVLMGDG LTIQEGSSVK ATGRIAQIPV SEAYLGRVVN ALAKPIDGRG
     EIAASEFRLI ESPAPGIISR RSVYEPLQTG LIAIDSMIPV GRGQRELIIG DRQTGKTAVA
     TDTILNQKGQ NVICVYVAIG QKASSVAQVV TNFQERGAME YTIVVAETAD SPATLQYLAP
     YTGAALAEYF MYRERHTSII YDDLSKQAQA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE
     RAAKSSSRLG EGSMTALPIV ETQSGDVSAY IPTNVISITD GQIFLSADLF NAGIRPAINV
     GISVSRVGSA AQIKAMKQVA GKSKLELAQF AELEAFAQFA SDLDKATQNQ LARGKRLREL
     LKQSQSEPLA VDEQVVTIYT GTNGYLDTLE IGQVKEFLVK LRTYLKKNKP QFQEIISSTK
     TFTEEAEALL KEAIQEQLEL FLLQEQ
//
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