ID F0GW82_9FIRM Unreviewed; 585 AA.
AC F0GW82;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=V-type ATP synthase alpha chain {ECO:0000256|HAMAP-Rule:MF_00309};
DE EC=7.1.2.2 {ECO:0000256|HAMAP-Rule:MF_00309};
DE AltName: Full=V-ATPase subunit A {ECO:0000256|HAMAP-Rule:MF_00309};
GN Name=atpA {ECO:0000256|HAMAP-Rule:MF_00309};
GN ORFNames=HMPREF9290_0450 {ECO:0000313|EMBL:EGC81980.1};
OS Anaerococcus prevotii ACS-065-V-Col13.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Anaerococcus.
OX NCBI_TaxID=879305 {ECO:0000313|EMBL:EGC81980.1, ECO:0000313|Proteomes:UP000005286};
RN [1] {ECO:0000313|EMBL:EGC81980.1, ECO:0000313|Proteomes:UP000005286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-065-V-Col13 {ECO:0000313|EMBL:EGC81980.1,
RC ECO:0000313|Proteomes:UP000005286};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. The V-type alpha chain is a catalytic subunit.
CC {ECO:0000256|HAMAP-Rule:MF_00309}.
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:0000256|HAMAP-Rule:MF_00309};
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|HAMAP-Rule:MF_00309}.
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:EGC81980.1}.
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DR EMBL; AEXM01000026; EGC81980.1; -; Genomic_DNA.
DR RefSeq; WP_004835026.1; NZ_AEXM01000026.1.
DR AlphaFoldDB; F0GW82; -.
DR STRING; 879305.HMPREF9290_0450; -.
DR PATRIC; fig|879305.3.peg.1063; -.
DR eggNOG; COG1155; Bacteria.
DR Proteomes; UP000005286; Unassembled WGS sequence.
DR GO; GO:0045259; C:proton-transporting ATP synthase complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IEA:UniProtKB-UniRule.
DR CDD; cd18111; ATP-synt_V_A-type_alpha_C; 1.
DR CDD; cd01134; V_A-ATPase_A; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00309; ATP_synth_A_arch; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR031686; ATP-synth_a_Xtn.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
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; IPR024034; ATPase_F1/V1_b/a_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022878; V-ATPase_asu.
DR PANTHER; PTHR43607; V-TYPE PROTON ATPASE CATALYTIC SUBUNIT A; 1.
DR PANTHER; PTHR43607:SF1; V-TYPE PROTON ATPASE CATALYTIC SUBUNIT A; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR Pfam; PF16886; ATP-synt_ab_Xtn; 1.
DR SMART; SM00382; AAA; 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.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP-
KW Rule:MF_00309};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00309}; Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_00309};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW Rule:MF_00309};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00309}; Reference proteome {ECO:0000313|Proteomes:UP000005286};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW Rule:MF_00309};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00309}.
FT DOMAIN 223..411
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 231..238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00309"
SQ SEQUENCE 585 AA; 65063 MW; 2B5B66A633B89233 CRC64;
MNKGKITKVS GPLIEAEGLS DANIYDVVEV SKDKLIGEII EMRGDVASIQ VYEETTGIGP
GDEVVSTGHP LSVELGPGML ERMYDGIQRP LEKLEDLAGE FLTRGVTSPA LDRDRVWEFN
PTASVSDKVE AGDIIGEVEE TSVITHKIMI PLGISGTIKD IKAGEFKVDE TIAVIETEDG
DKEVTMVQKW PVRTARPSKR KLDPNEPLIT GQRVIDTFFP VAKGGTAAIP GPFGSGKTVV
QHQIAKYADA DIVIYVGCGE RGNEMTDVLN EFPELIDPKT GESIMKRTVL IANTSNMPVA
AREASIYTGI TLAEYFRDMG YNVAMMADST SRWAEALREM SGRLEEMPGD EGFPAYLASR
IADFYERAGK VEVLGSRDDI GSLSVIGAVS PPGGDLSEPV TQATLRIVKV FWGLDYDLSY
QRHFPAINWL SSYSLYQDKM DKYIDSEVDE DFSKNRKRSM SLLQQESGLQ EVVRLVGRDA
LSDDDKLKLD VTKSIREDYL QQNAFHDVDT YCSLKKQDKM LNVILYNYDK SLEALSNGVE
LEDIEKLPVR ERITRLKLIS EDDMDQINEI RSEIDKQIDE LIREA
//
