VATA_SULTO
ID VATA_SULTO Reviewed; 592 AA.
AC Q971B7; F9VNC6; P09639;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=V-type ATP synthase alpha chain;
DE EC=7.1.2.2;
DE AltName: Full=Sul-ATPase alpha chain;
DE AltName: Full=V-ATPase subunit A;
GN Name=atpA; OrderedLocusNames=STK_14360;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-41 AND 65-81.
RX PubMed=2896191; DOI=10.1016/s0021-9258(18)68740-x;
RA Denda K., Konishi J., Oshima T., Date T., Yoshida M.;
RT "The membrane-associated ATPase from Sulfolobus acidocaldarius is distantly
RT related to F1-ATPase as assessed from the primary structure of its alpha-
RT subunit.";
RL J. Biol. Chem. 263:6012-6015(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
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 -!- 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 -!- SUBUNIT: Sul-ATPase is composed of six (or maybe five) subunits: alpha,
CC beta, delta, gamma, C (proteolipid), and possibly epsilon.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally reported as originating from S.acidocaldarius.
CC {ECO:0000305|PubMed:2896191}.
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DR EMBL; J03218; AAA72192.1; -; Genomic_DNA.
DR EMBL; BA000023; BAK54572.1; -; Genomic_DNA.
DR PIR; A28652; A28652.
DR RefSeq; WP_052846566.1; NC_003106.2.
DR AlphaFoldDB; Q971B7; -.
DR SMR; Q971B7; -.
DR STRING; 273063.STK_14360; -.
DR PRIDE; Q971B7; -.
DR EnsemblBacteria; BAK54572; BAK54572; STK_14360.
DR GeneID; 1459467; -.
DR KEGG; sto:STK_14360; -.
DR PATRIC; fig|273063.9.peg.1636; -.
DR eggNOG; arCOG00868; Archaea.
DR OMA; RIVKTFW; -.
DR OrthoDB; 6736at2157; -.
DR BRENDA; 7.1.2.2; 15396.
DR Proteomes; UP000001015; Chromosome.
DR GO; GO:0033178; C:proton-transporting two-sector ATPase complex, catalytic domain; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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 Gene3D; 1.10.1140.10; -; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 3.40.50.300; -; 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; IPR005726; ATP_synth_asu_arc.
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; PTHR43607; 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; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01043; ATP_syn_A_arch; 1.
PE 1: Evidence at protein level;
KW ATP synthesis; ATP-binding; Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Nucleotide-binding;
KW Reference proteome; Translocase; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2896191"
FT CHAIN 2..592
FT /note="V-type ATP synthase alpha chain"
FT /id="PRO_0000144607"
FT BINDING 234..241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 483
FT /note="S -> E (in Ref. 1; AAA72192)"
FT /evidence="ECO:0000305"
FT CONFLICT 505
FT /note="Q -> E (in Ref. 1; AAA72192)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 592 AA; 66098 MW; CEF76C105C206C80 CRC64;
MVSEGRVVRV NGPLVIADGM REAQMFEVVY VSDLKLVGEI TRIEGDRAFI QVYESTDGVK
PGDKVYRSGA PLSVELGPGL IGKIYDGLQR PLDSIAKVSN SPFVARGVSI PALDRQTKWH
FVPKVKSGDK VGPGDIIGVV QETDLIEHRI LIPPNVHGTL KELAREGDYT VEDVVAVVDM
NGDEIPVKMY QKWPVRIPRP YKEKLEPVEP LLTGIRVLDT VFPIAKGGTA AIPGPFGSGK
TVTLQSLAKW SAAKVVIYVG CGERGNEMTD ELRSFPKLKD PWTGKPLLLR TILVANTSNM
PVAARESSIY VGVTMAEYFR DQGYDVLLVA DSTSRWAEAL RDLGGRMEEM PAEEGFPSYL
PSRLAEYYER AGRVIALGNP ERYGSVTIAS AVSPPGGDFT EPVTSNTLRF VRVFWPLDVS
LAQARHYPAI NWIQGFSAYV DLVAQWWHKN VDPNWKEMRD TMMKVLIRED ELRQIVRLVG
PESLAEKDKL VLEAAKLIKD AFLKQNAYDD IDAFSSPQKQ VRIMRLIYIF YNQSQDLISK
GVPLKKILDK VGPIEPEIIR IKYTIKNDEL NKIDEIENKL KATFDSLLKE VS
