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Database: UniProt
Entry: Q2L368_9LACO
LinkDB: Q2L368_9LACO
Original site: Q2L368_9LACO 
ID   Q2L368_9LACO            Unreviewed;       353 AA.
AC   Q2L368;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   13-SEP-2023, entry version 82.
DE   SubName: Full=ATP synthase alpha subunit {ECO:0000313|EMBL:CAJ43382.1};
DE            EC=3.6.3.14 {ECO:0000313|EMBL:CAJ33226.1};
DE   Flags: Fragment;
GN   Name=atpA {ECO:0000313|EMBL:CAJ43382.1};
OS   Lactobacillus gallinarum.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=52242 {ECO:0000313|EMBL:CAJ43382.1};
RN   [1] {ECO:0000313|EMBL:CAJ33226.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Type strain: LMG 9435 {ECO:0000313|EMBL:CAJ33226.1};
RA   Naser S.M., Vancanneyt M., Hoste B., Dawyndt P., Gevers D., Cleenwerck I.,
RA   Swings J.;
RT   "Development of a rapid and broadly applicable multilocus sequence analysis
RT   (MLSA)-based identification approach for the Lactobacillus genus using
RT   pheS, rpoA and atpA genes.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAJ43382.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Type strain: LMG 9435 {ECO:0000313|EMBL:CAJ43382.1};
RA   Naser S.M., Hagen K.E., Vancanneyt M., Cleewerck I., Swings J.,
RA   Tompkins T.A.;
RT   "Lactobacillus suntoryeus Cachat and Priest 2005 is a later synonym of
RT   Lactobacillus helveticus (Orla-Jensen 1919) Bergey et al. 1925 (Approved
RT   Lists 1980).";
RL   Int. J. Syst. Evol. Microbiol. 56:355-360(2006).
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:0000256|ARBA:ARBA00003784}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936}.
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DR   EMBL; AM087874; CAJ33226.1; -; Genomic_DNA.
DR   EMBL; AM157789; CAJ43382.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2L368; -.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR   CDD; cd01132; F1-ATPase_alpha_CD; 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   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   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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   CF(1) {ECO:0000256|ARBA:ARBA00023196};
KW   Hydrolase {ECO:0000313|EMBL:CAJ33226.1};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          2..39
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02874"
FT   DOMAIN          96..311
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT                   nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00006"
FT   DOMAIN          318..353
FT                   /note="ATP synthase alpha subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00306"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAJ43382.1"
FT   NON_TER         353
FT                   /evidence="ECO:0000313|EMBL:CAJ43382.1"
SQ   SEQUENCE   353 AA;  38105 MW;  D812296603EEEC90 CRC64;
     KFDNGSYGIA QNLDASDVGI IILGKFDDIR EGDRVQRTGR IMSVPVGDAL IGRVVNPLGQ
     PVDGLGEIKA DKTRPIEEKA PGVMDRQSVN QPLQTGIKAI DALVPIGRGQ RELIIGDRKT
     GKTSLAIDTI LNQKNQDVIC IYVAIGQKES TVRTQVETLK RFGAMDYTIV VEAGPSEPAP
     MLYIAPYAGT AMGEEFMYNG KDVLIVFDDL SKQAVAYREL SLLLRRPPGR EAYPGDVFYL
     HSRLLERSAK LSDKLGGGSL TALPIIQTEA GDISAYIPTN VISITDGQIF LQSDLFFAGT
     RPAIDAGNSV SRVGGNAQIK AMKKVAGTLR TDLAAFRELE SFAQFGSDLD QAT
//
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