ID S2EQT3_9ARCH Unreviewed; 592 AA.
AC S2EQT3;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=V-type ATP synthase alpha chain {ECO:0000256|ARBA:ARBA00018003, ECO:0000256|HAMAP-Rule:MF_00309};
DE EC=7.1.2.2 {ECO:0000256|ARBA:ARBA00012473, ECO:0000256|HAMAP-Rule:MF_00309};
DE AltName: Full=V-ATPase subunit A {ECO:0000256|ARBA:ARBA00031719, ECO:0000256|HAMAP-Rule:MF_00309};
GN Name=atpA {ECO:0000256|HAMAP-Rule:MF_00309};
GN ORFNames=BG20_I0030 {ECO:0000313|EMBL:EPA06812.1};
OS Candidatus Nitrosarchaeum limnium BG20.
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC Nitrosopumilaceae; Nitrosarchaeum.
OX NCBI_TaxID=859192 {ECO:0000313|EMBL:EPA06812.1, ECO:0000313|Proteomes:UP000014065};
RN [1] {ECO:0000313|EMBL:EPA06812.1, ECO:0000313|Proteomes:UP000014065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BG20 {ECO:0000313|EMBL:EPA06812.1,
RC ECO:0000313|Proteomes:UP000014065};
RX PubMed=22461554; DOI=10.1128/JB.00007-12;
RA Mosier A.C., Allen E.E., Kim M., Ferriera S., Francis C.A.;
RT "Genome Sequence of "Candidatus Nitrosoarchaeum limnia" BG20, a Low-
RT Salinity Ammonia-Oxidizing Archaeon from the San Francisco Bay Estuary.";
RL J. Bacteriol. 194:2119-2120(2012).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. The archaeal alpha chain is a catalytic subunit.
CC {ECO:0000256|ARBA:ARBA00003912, 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|ARBA:ARBA00001741, ECO:0000256|HAMAP-
CC 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:EPA06812.1}.
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DR EMBL; AHJG01000010; EPA06812.1; -; Genomic_DNA.
DR RefSeq; WP_010189545.1; NZ_AHJG01000010.1.
DR AlphaFoldDB; S2EQT3; -.
DR PATRIC; fig|859192.6.peg.82; -.
DR OrthoDB; 115235at2157; -.
DR Proteomes; UP000014065; Unassembled WGS sequence.
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; cd18119; ATP-synt_V_A-type_alpha_N; 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; 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; 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.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 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:UP000014065};
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 226..414
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 234..241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00309"
SQ SEQUENCE 592 AA; 65156 MW; 26A3F23120F77E0D CRC64;
MAAQGRIVWV SGPAVKADGM SDAKMYETVV VGNSKLVGEV IRLTGDVAFI QVYESTSGLK
PGEPVVGTGN PLSVLLGPGI IGQIYDGIQR PLKELSKVSG SFIGRGITTT PVDMVKKYHF
VPSVSNGDVI AAGNVLGTVQ ETDLITNSIL VPPDHPGGKI SNVVSEGDYD LETVLCTSEK
DGQKIPLKMY HRWPVRKPRP YHTRYDPTVP LLTGQRVIDT FFPIAKGGTG SIPGAFGTGK
TVTLHQIAKW ADSQVVVYIG CGERGNEMTE VLVEFPHLKD PRSGKPLMDR TVLVANTSNM
PVAAREASIY TGVTIAEYYR DMGYDVVLVA DSTSRWAESL REMSGRLEEM PAEEGYPSYL
ASRLAEFYER AGRVKAIGSP DRDGSVTLVG AVSPSGGDFT EPVTTHTMRF IKTFWALDAK
LAYSRHYPSI NWMNSYSGYL GDIAKWWTEN INSDWLSLRS EAYGVLQRED TLKEIVRLLG
PEALPDEEKL ILEVARMVKI GHLQQNSFDD VDTYCSPQKQ YKLLKLLVEF YRRGQQALKE
GASLADIRAL AIVSTLLKAR MDIKDNEMAK LDQLDIDMKE QFKSITGVKV SN
//
