ATPA_MAIZE
ID ATPA_MAIZE Reviewed; 507 AA.
AC P05022;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=ATP synthase subunit alpha, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01346};
DE EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01346};
DE AltName: Full=ATP synthase F1 sector subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
DE AltName: Full=F-ATPase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
GN Name=atpA {ECO:0000255|HAMAP-Rule:MF_01346};
OS Zea mays (Maize).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2885245; DOI=10.1093/genetics/116.1.127;
RA Rodermel S.R., Bogorao L.;
RT "Molecular evolution and nucleotide sequences of the maize plastid genes
RT for the alpha subunit of CF1 (atpA) and the proteolipid subunit of CF0
RT (atpH).";
RL Genetics 116:127-139(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=7666415; DOI=10.1006/jmbi.1995.0460;
RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.;
RT "Complete sequence of the maize chloroplast genome: gene content, hotspots
RT of divergence and fine tuning of genetic information by transcript
RT editing.";
RL J. Mol. Biol. 251:614-628(1995).
RN [3]
RP PROTEIN SEQUENCE OF 378-384, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT
RP SER-383.
RC STRAIN=cv. Olenka; TISSUE=Bundle sheath cell, and Mesophyll cell;
RX PubMed=22833285; DOI=10.1002/pmic.201200196;
RA Fristedt R., Wasilewska W., Romanowska E., Vener A.V.;
RT "Differential phosphorylation of thylakoid proteins in mesophyll and bundle
RT sheath chloroplasts from maize plants grown under low or high light.";
RL Proteomics 12:2852-2861(2012).
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:0000255|HAMAP-Rule:MF_01346}.
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:0000255|HAMAP-Rule:MF_01346};
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:0000255|HAMAP-Rule:MF_01346}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01346, ECO:0000269|PubMed:22833285};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01346}.
CC -!- PTM: Only phosphorylated in mesophyll cells, and only when cells are
CC grown under high rather than low light regimes (70 vs 900 umol
CC photons/m-2/s). {ECO:0000269|PubMed:22833285}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01346}.
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DR EMBL; X05255; CAA28876.1; -; Genomic_DNA.
DR EMBL; M27557; AAA84474.1; -; Genomic_DNA.
DR EMBL; X86563; CAA60283.1; -; Genomic_DNA.
DR PIR; S06291; PWZMA.
DR RefSeq; NP_043022.1; NC_001666.2.
DR AlphaFoldDB; P05022; -.
DR SMR; P05022; -.
DR iPTMnet; P05022; -.
DR PRIDE; P05022; -.
DR GeneID; 845169; -.
DR KEGG; zma:845169; -.
DR MaizeGDB; 69206; -.
DR OrthoDB; 470054at2759; -.
DR Proteomes; UP000007305; Chloroplast.
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); IBA:GO_Central.
DR GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR CDD; cd18113; ATP-synt_F1_alpha_C; 1.
DR CDD; cd01132; F1_ATPase_alpha; 1.
DR Gene3D; 1.20.150.20; -; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 3.40.50.300; -; 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.
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 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; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00962; atpA; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW ATP synthesis; ATP-binding; CF(1); Chloroplast; Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Nucleotide-binding;
KW Phosphoprotein; Plastid; Reference proteome; Thylakoid; Translocase;
KW Transport.
FT CHAIN 1..507
FT /note="ATP synthase subunit alpha, chloroplastic"
FT /id="PRO_0000144379"
FT BINDING 170..177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT SITE 363
FT /note="Required for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22833285"
SQ SEQUENCE 507 AA; 55707 MW; 44685BF464B6302E CRC64;
MATLRVDEIN KILRERIEQY NRKVGIENIG RVVQVGDGIA RIIGLGEIMS GELVEFAEGT
RGIALNLESK NVGIVLMGDG LMIQEGSFVK ATGRIAQIPV SEAYLGRVIN ALAKPIDGRG
EIVASESRLI ESPAPGIISR RSVYEPLQTG LIAIDSMIPI GRGQRELIIG DRQTGKTAVA
TDTILNQKGQ DVICVYVAIG QRASSVAQVV TTFHEEGAME YTIVVAEMAD SPATLQYLAP
YTGAALAEYF MYRERHTLII YDDLSKQAQA YRQMSLLLRR PPGREAYLGD VFYLHSRLLE
RAAKLNSLLG EGSMTALPIV ETQSGDVSAY IPTNVISITD GQIFLSADLF NAGIRPAINV
GISVSRVGSA AQIKAMKQVA GKSKLELAQF AELQAFAQFA SALDKTSQNQ LARGRRLREL
LKQSQSNPLP VEEQVATIYT GTRGYLDSLE IEQVKKFLDE LRKHLKDTKP QFQEIISSSK
TFTEQAETLL KEAIQEQLER FSLQEQT
