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Database: UniProt
Entry: A9JQB0_9LACO
LinkDB: A9JQB0_9LACO
Original site: A9JQB0_9LACO 
ID   A9JQB0_9LACO            Unreviewed;       341 AA.
AC   A9JQB0;
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:CAP16930.1};
DE   Flags: Fragment;
GN   Name=atpA {ECO:0000313|EMBL:CAP16930.1};
OS   Pediococcus inopinatus.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Pediococcus.
OX   NCBI_TaxID=114090 {ECO:0000313|EMBL:CAP16930.1};
RN   [1] {ECO:0000313|EMBL:CAP16930.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LAB 1451 {ECO:0000313|EMBL:CAP16930.1};
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; AM899927; CAP16930.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9JQB0; -.
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..57
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02874"
FT   DOMAIN          114..329
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:CAP16930.1"
FT   NON_TER         341
FT                   /evidence="ECO:0000313|EMBL:CAP16930.1"
SQ   SEQUENCE   341 AA;  36729 MW;  C555396E126D89A4 CRC64;
     DGIARAHGLD NALAGELLEF SNGVYGMVQN LESNDVGIVI LGGYDDIREG DTVKRTGRIM
     EVPVGDALVG RVVNTLGQPI DGKGEIKTDH TRPVERKAPG VMERQSVSEP LQTGIKAIDA
     LVPIGRGQRE LIIGDRKTGK TSLAIDTILN QKDQNIICIY VAIGQKESTV RTQVDTLEKY
     GAMDYTIVLS AGPSEPAPML YLAPYAGAAM GEEFMFNGKH VLIVYDDLSK QADAYRELSL
     ILRRPPGREA YPGDIFYTHS RLLERAAKLN DELGAGSMTA LPFVETKAGD IAAYIPTNVI
     SITDGQIFLD SDLFYSGTRP AIDAGSSVSR VGGDAQIKAM K
//
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