ID A0A2J7ZXM5_9CHLO Unreviewed; 571 AA.
AC A0A2J7ZXM5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 28-JAN-2026, entry version 26.
DE RecName: Full=ATP synthase subunit alpha {ECO:0000256|RuleBase:RU003551};
GN ORFNames=TSOC_008746 {ECO:0000313|EMBL:PNH05017.1};
OS Tetrabaena socialis.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Tetrabaenaceae; Tetrabaena.
OX NCBI_TaxID=47790 {ECO:0000313|EMBL:PNH05017.1, ECO:0000313|Proteomes:UP000236333};
RN [1] {ECO:0000313|EMBL:PNH05017.1, ECO:0000313|Proteomes:UP000236333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-571 {ECO:0000313|EMBL:PNH05017.1,
RC ECO:0000313|Proteomes:UP000236333};
RX PubMed=29294063; DOI=10.1093/molbev/msx332;
RA Featherston J., Arakaki Y., Hanschen E.R., Ferris P.J., Michod R.E.,
RA Olson B.J.S.C., Nozaki H., Durand P.M.;
RT "The 4-celled Tetrabaena socialis nuclear genome reveals the essential
RT components for genetic control of cell number at the origin of
RT multicellularity in the volvocine lineage.";
RL Mol. Biol. Evol. 0:0-0(2017).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC Complex V) produces ATP from ADP in the presence of a proton gradient
CC across the membrane which is generated by electron transport complexes
CC of the respiratory chain. F-type ATPases consist of two structural
CC domains, F(1) - containing the extramembraneous catalytic core, and
CC 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. Subunits alpha and
CC beta form the catalytic core in F(1). Rotation of the central stalk
CC against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of
CC ATP in three separate catalytic sites on the beta subunits. Subunit
CC alpha does not bear the catalytic high-affinity ATP-binding sites.
CC {ECO:0000256|ARBA:ARBA00037296}.
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. {ECO:0000256|RuleBase:RU003551}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|ARBA:ARBA00004273}.
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:PNH05017.1}.
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DR EMBL; PGGS01000341; PNH05017.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J7ZXM5; -.
DR OrthoDB; 30023at2759; -.
DR Proteomes; UP000236333; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045259; C:proton-transporting ATP synthase complex; IEA:UniProtKB-KW.
DR GO; GO:0043531; F:ADP binding; IEA:TreeGrafter.
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; 1.
DR CDD; cd18116; ATP-synt_F1_alpha_N; 1.
DR CDD; cd01132; F1-ATPase_alpha_CD; 1.
DR FunFam; 1.20.150.20:FF:000001; ATP synthase subunit alpha; 1.
DR FunFam; 3.40.50.300:FF:002432; ATP synthase subunit alpha, mitochondrial; 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 NCBIfam; NF009884; PRK13343.1; 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 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:RU003551};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003551};
KW CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|RuleBase:RU003551};
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 Mitochondrion {ECO:0000256|ARBA:ARBA00022792};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003551};
KW Reference proteome {ECO:0000313|Proteomes:UP000236333};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000339}.
FT DOMAIN 94..158
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 215..438
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
FT DOMAIN 445..565
FT /note="ATP synthase alpha subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00306"
SQ SEQUENCE 571 AA; 61531 MW; 6D0A69D591A7108A CRC64;
MRNSALSFVR AGVLQLGSQS GASLLAQEGA STLSKRAEQA ILHAARAFAS DSKALDELRK
PKFTSKYLIN HVSEKLIPAV KEWEKQYQPP VIHLGRVLSV GDGIARIYGL KSVQAGELVC
FDCGVKGMAL NLQADHVGVV VFGNDSLIHQ GDLVYRTGQI VNVPIGPGTL GRVVDALGQP
IDGKGPLLNV KSSLVEVKAP GIIARQSVRE PLYTGVKAVD ALVPIGRGQR ELIIGDRQTG
KTAIAVDCIL HQTHLNGITS RKNRVYCIYV AIGQKRSTVA QLVKMFGAAG ALRYTIIVSA
TASDAAPLQF LAPYSGCAMA EYFRDNGKHA VIIYDDLSKQ SVAYRQMSLL LRRPPGREAF
PGDVFYLHSR LLERAAKMSL AMGGGSLTAF PVIETQAGDV SAYIATNVIS ITDGQIFLET
ELFYKGIRPA LNVGLSVSRV GSAAQFPGMK QVAGTLKLEL AQYREVAAFA QFGSDLDAAT
QYVLERGARL TEVLKQKQFA PMDIELQTVL VYAATKGYLD KVPVNQITGC EEVILKHIDP
KIFKILKAQG KISPAVNAHL AQQMSNLPLA K
//
