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VATD_DEIDV
ID   VATD_DEIDV              Reviewed;         224 AA.
AC   C1CXU5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=V-type ATP synthase subunit D {ECO:0000255|HAMAP-Rule:MF_00271};
DE   AltName: Full=V-ATPase subunit D {ECO:0000255|HAMAP-Rule:MF_00271};
GN   Name=atpD {ECO:0000255|HAMAP-Rule:MF_00271}; OrderedLocusNames=Deide_01010;
OS   Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=546414;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115;
RX   PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA   de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA   Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA   Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT   "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT   bacterium Deinococcus deserti.";
RL   PLoS Genet. 5:E1000434-E1000434(2009).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. {ECO:0000255|HAMAP-Rule:MF_00271}.
CC   -!- SIMILARITY: Belongs to the V-ATPase D subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_00271}.
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DR   EMBL; CP001114; ACO44901.1; -; Genomic_DNA.
DR   RefSeq; WP_012692024.1; NC_012526.1.
DR   AlphaFoldDB; C1CXU5; -.
DR   SMR; C1CXU5; -.
DR   STRING; 546414.Deide_01010; -.
DR   PaxDb; C1CXU5; -.
DR   EnsemblBacteria; ACO44901; ACO44901; Deide_01010.
DR   KEGG; ddr:Deide_01010; -.
DR   eggNOG; COG1394; Bacteria.
DR   HOGENOM; CLU_069688_2_1_0; -.
DR   OMA; SKNIMGV; -.
DR   OrthoDB; 1334900at2; -.
DR   Proteomes; UP000002208; 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   3: Inferred from homology;
KW   ATP synthesis; Hydrogen ion transport; Ion transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..224
FT                   /note="V-type ATP synthase subunit D"
FT                   /id="PRO_1000209790"
FT   REGION          205..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   224 AA;  24147 MW;  46F516819699E7F8 CRC64;
     MAGQISPTRS ALLASKASLK TASGGADLLK RKRDALIGEF FALVKDALAA REQLGGVSKG
     AYTSLFGAKA WDSPEAVESL SLAGSGDYAV NMQIESIYGV KVPRINIPER TQTTNFSPIN
     VGARTIQAAT DFGGVMEAIV KVAATETKLR RIGEEIKKTS RRVNALEQVV IPGIEDDIRF
     IRSVLDQRER EASYTQKKIK AKIEAKAKQQ RKDIQSGNHG SAAD
 
 
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