VATD_SULTO
ID VATD_SULTO Reviewed; 216 AA.
AC P62017; F9VNC8; P22721; P62016;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=V-type ATP synthase subunit D;
DE AltName: Full=Sul-ATPase gamma chain;
DE AltName: Full=V-ATPase subunit D;
GN Name=atpD; Synonyms=atpG; OrderedLocusNames=STK_14380;
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 201-210.
RX PubMed=2147683; DOI=10.1016/s0021-9258(18)45768-7;
RA Denda K., Konishi J., Hajiro K., Oshima T., Date T., Yoshida M.;
RT "Structure of an ATPase operon of an acidothermophilic archaebacterium,
RT Sulfolobus acidocaldarius.";
RL J. Biol. Chem. 265:21509-21513(1990).
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.
CC -!- SUBUNIT: Sul-ATPase is composed of six (or maybe five) subunits: alpha,
CC beta, delta, gamma, C (proteolipid), and possibly epsilon.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the V-ATPase D subunit family. {ECO:0000305}.
CC -!- CAUTION: Was originally reported as originating from S.acidocaldarius.
CC {ECO:0000305|PubMed:2147683}.
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DR EMBL; M57238; AAA72941.1; ALT_TERM; Genomic_DNA.
DR EMBL; BA000023; BAK54574.1; -; Genomic_DNA.
DR PIR; B36493; B36493.
DR RefSeq; WP_010979483.1; NC_003106.2.
DR AlphaFoldDB; P62017; -.
DR SMR; P62017; -.
DR STRING; 273063.STK_14380; -.
DR EnsemblBacteria; BAK54574; BAK54574; STK_14380.
DR GeneID; 1459469; -.
DR KEGG; sto:STK_14380; -.
DR PATRIC; fig|273063.9.peg.1638; -.
DR eggNOG; arCOG04101; Archaea.
DR OMA; SKNIMGV; -.
DR OrthoDB; 93236at2157; -.
DR Proteomes; UP000001015; Chromosome.
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:InterPro.
DR GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00271; ATP_synth_D_arch; 1.
DR InterPro; IPR002699; V_ATPase_D.
DR PANTHER; PTHR11671; PTHR11671; 1.
DR Pfam; PF01813; ATP-synt_D; 1.
DR TIGRFAMs; TIGR00309; V_ATPase_subD; 1.
PE 1: Evidence at protein level;
KW ATP synthesis; Direct protein sequencing; Hydrogen ion transport;
KW Ion transport; Reference proteome; Transport.
FT CHAIN 1..216
FT /note="V-type ATP synthase subunit D"
FT /id="PRO_0000144260"
SQ SEQUENCE 216 AA; 25105 MW; 344131AE21B67CE2 CRC64;
MSSRKILPTK LNLINLRKQI RLTRTIKRLL ENKREVLLIY LREYANEYEK LYSEVSQLLK
EVYETYLMGV SAEGISTVES YANSVPPSLQ VKSDLKVLFG VRIPIVKLDE NSIQPQPFGD
IEVSPYITKS RDAIAEAFKK ILELVEMESA IRSLSTELRK TQRLINAIDS YILPYYTSSA
KYIKGVLDDR TREEFVRLKM IRKVLQRRRG ENVGNR