ID   A9JQB3_9LACO            Unreviewed;       337 AA.
AC   A9JQB3;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=ATP synthase alpha subunit {ECO:0000313|EMBL:CAP16933.1};
DE   Flags: Fragment;
GN   Name=atpA {ECO:0000313|EMBL:CAP16933.1};
OS   Pediococcus parvulus.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Pediococcus.
OX   NCBI_TaxID=54062 {ECO:0000313|EMBL:CAP16933.1};
RN   [1] {ECO:0000313|EMBL:CAP16933.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LAB 299 {ECO:0000313|EMBL:CAP16933.1};
RA   De Bruyne K., Franz C.M., Vancanneyt M., Schillinger U., Mozzi F.,
RA   de Valdez G.F., De Vuyst L., Vandamme P.;
RT   "Pediococcus argentinicus sp. nov. from Argentinean fermented wheat flour
RT   and identification of Pediococcus species by pheS, rpoA and atpA sequence
RT   analysis.";
RL   Int. J. Syst. Evol. Microbiol. 58:2909-2916(2008).
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936}.
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DR   EMBL; AM899930; CAP16933.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9JQB3; -.
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:InterPro.
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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR023366; ATP_synth_asu-like_sf.
DR   InterPro; IPR033732; ATP_synth_F1_a_nt-bd_dom.
DR   InterPro; IPR005294; ATP_synth_F1_asu.
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; PF02874; ATP-synt_ab_N; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..55
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02874"
FT   DOMAIN          112..327
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT                   nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00006"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAP16933.1"
FT   NON_TER         337
FT                   /evidence="ECO:0000313|EMBL:CAP16933.1"
SQ   SEQUENCE   337 AA;  36380 MW;  4089716C87D8FBFF CRC64;
     IARAHGLDNA LAGELLEFSN GVYGMVQNLE SNDVGIVILG NYDDIREGDT VKRTGRIMEV
     PVGEALIGRV VNTLGQPIDG KGEIKTDHTR PVERKAPGVM ERQSVSEPLQ TGIKAIDSLV
     PIGRGQRELI IGDRKTGKTS LAIDTILNQK NQNIICIYVA IGQKESTVRT QVDTLEKFGA
     MDYTIVLSAG PSEPAPMLYL APYAGAAMGE EFMFNGKHVL IVYDDLSKQA DAYRELSLIL
     RRPPGREAYP GDIFYTHSRL LERAAKLNDK LGAGSMTALP FVETKAGDIA AYIPTNVISI
     TDGQIFLDSD LFYSGTRPAI DAGSSVSRVG GDAQIKA
//