ATPA_CHLRE
ID ATPA_CHLRE Reviewed; 508 AA.
AC P26526; B7U1L0;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=ATP synthase subunit alpha, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01346, ECO:0000303|PubMed:8543042};
DE EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01346, ECO:0000269|PubMed:8543042};
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, ECO:0000303|PubMed:8543042};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=19473533; DOI=10.1186/1471-2148-9-120;
RA Smith D.R., Lee R.W.;
RT "Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome:
RT addressing the mutational-hazard hypothesis.";
RL BMC Evol. Biol. 9:120-120(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-112.
RX PubMed=6302265; DOI=10.1016/0022-2836(82)90547-2;
RA Dron M., Rahire M., Rochaix J.-D.;
RT "Sequence of the chloroplast DNA region of Chlamydomonas reinhardii
RT containing the gene of the large subunit of ribulose bisphosphate
RT carboxylase and parts of its flanking genes.";
RL J. Mol. Biol. 162:775-793(1982).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 55-508.
RC STRAIN=137c / CC-125;
RX PubMed=1531617; DOI=10.1007/bf00040681;
RA Leu S., Schlesinger J., Michaels A., Shavit N.;
RT "Complete DNA sequence of the Chlamydomonas reinhardtii chloroplast atpA
RT gene.";
RL Plant Mol. Biol. 18:613-616(1992).
RN [4]
RP PROTEIN SEQUENCE OF 2-13, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cw15;
RX PubMed=8543042; DOI=10.1016/0014-5793(95)01332-6;
RA Fiedler H.R., Schmid R., Leu S., Shavit N., Strotmann H.;
RT "Isolation of CF0CF1 from Chlamydomonas reinhardtii cw15 and the N-terminal
RT amino acid sequences of the CF0CF1 subunits.";
RL FEBS Lett. 377:163-166(1995).
RN [5]
RP IDENTIFICATION, AND COMPLETE PLASTID GENOME.
RX PubMed=12417694; DOI=10.1105/tpc.006155;
RA Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W., Harris E.H.,
RA Stern D.B.;
RT "The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a
RT sea of repeats.";
RL Plant Cell 14:2659-2679(2002).
CC -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence
CC of a proton or sodium gradient. F-type ATPases consist of two
CC structural domains, F(1) containing the extramembraneous catalytic core
CC and F(0) containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation.
CC {ECO:0000269|PubMed:8543042}.
CC -!- FUNCTION: The alpha chain is a regulatory subunit.
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 ECO:0000269|PubMed:8543042};
CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core
CC - and F(0) - the membrane proton channel. F(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has four main
CC subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains
CC form an alternating ring which encloses part of the gamma chain. F(1)
CC is attached to F(0) by a central stalk formed by the gamma and epsilon
CC chains, while a peripheral stalk is formed by the delta, b and b'
CC chains. {ECO:0000269|PubMed:8543042}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01346, ECO:0000269|PubMed:8543042};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01346}.
CC -!- MISCELLANEOUS: In plastids the F-type ATPase is also known as
CC CF(1)CF(0). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01346}.
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DR EMBL; FJ423446; ACJ50157.1; -; Genomic_DNA.
DR EMBL; J01399; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X60298; CAA42840.1; -; Genomic_DNA.
DR EMBL; BK000554; DAA00951.1; -; Genomic_DNA.
DR PIR; A05002; PWKMA.
DR RefSeq; NP_958406.1; NC_005353.1.
DR AlphaFoldDB; P26526; -.
DR SMR; P26526; -.
DR STRING; 3055.DAA00951; -.
DR PaxDb; P26526; -.
DR PRIDE; P26526; -.
DR ProMEX; P26526; -.
DR GeneID; 2717041; -.
DR KEGG; cre:ChreCp050; -.
DR eggNOG; KOG1353; Eukaryota.
DR HOGENOM; CLU_010091_2_1_1; -.
DR InParanoid; P26526; -.
DR OrthoDB; 470054at2759; -.
DR Proteomes; UP000006906; 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 Plastid; Reference proteome; Thylakoid; Translocase; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8543042"
FT CHAIN 2..508
FT /note="ATP synthase subunit alpha, chloroplastic"
FT /id="PRO_0000144372"
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 VARIANT 438
FT /note="L -> I (in strain: CC-503)"
SQ SEQUENCE 508 AA; 54752 MW; 2173C94DB8C28412 CRC64;
MAMRTPEELS NLIKDLIEQY TPEVKMVDFG IVFQVGDGIA RIYGLEKAMS GELLEFEDGT
LGIALNLEAN NVGAVLLGDG LKITEGSRVR CTGKIAEIPV GEAYLGRVVD GLARPVDGKG
AVQTKDSRAI ESPAPGIVAR RSVYEPLATG LVAVDAMIPV GRGQRELIIG DRQTGKTAIA
VDTILNQKGK GVICVYVAIG QKASSVAQVL NTLKERGALD YTIIVMANAN EPATLQYLAP
YTGATLAEYF MYTGRPTLTI YDDLSKQAQA YREMSLLLRR PPGREAYPGD VFYLHSRLLE
RAAKLNNALG EGSMTALPIV ETQEGDVSAY IPTNVISITD GQIFLAAGLF NSGLRPAINV
GISVSRVGSA AQPKAMKQVA GKLKLELAQF AELEAFSQFA SDLDQATQNQ LARGARLREI
LKQPQSSPLS VEEQVASLYA GTNGYLDKLE VSQVRAYLSG LRSYLANSYP KYGEILRSTL
TFTPEAEGLV KQAINEYLEE FKSQAKAA
