ID   VATB_HALS3              Reviewed;         471 AA.
AC   B0R754;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=V-type ATP synthase beta chain {ECO:0000255|HAMAP-Rule:MF_00310};
DE   AltName: Full=V-ATPase subunit B {ECO:0000255|HAMAP-Rule:MF_00310};
GN   Name=atpB {ECO:0000255|HAMAP-Rule:MF_00310}; OrderedLocusNames=OE_3984R;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. The archaeal beta chain is a regulatory subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_00310}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255|HAMAP-Rule:MF_00310}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM774415; CAP14573.1; -; Genomic_DNA.
DR   RefSeq; WP_010903578.1; NC_010364.1.
DR   AlphaFoldDB; B0R754; -.
DR   SMR; B0R754; -.
DR   EnsemblBacteria; CAP14573; CAP14573; OE_3984R.
DR   GeneID; 5953672; -.
DR   KEGG; hsl:OE_3984R; -.
DR   HOGENOM; CLU_022916_0_0_2; -.
DR   OMA; MLMMDSV; -.
DR   PhylomeDB; B0R754; -.
DR   Proteomes; UP000001321; 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:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00310; ATP_synth_B_arch; 1.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR005724; ATPase_A1-cplx_bsu.
DR   InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR022879; V-ATPase_su_B/beta.
DR   PANTHER; PTHR43389; PTHR43389; 1.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   PIRSF; PIRSF039114; V-ATPsynth_beta/V-ATPase_B; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01041; ATP_syn_B_arch; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Hydrogen ion transport; Ion transport; Transport.
FT   CHAIN           1..471
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_1000115660"
SQ   SEQUENCE   471 AA;  51958 MW;  12DB1835E0EA9E62 CRC64;
     MKEYQTITEV SGPLVYVETD EPIGYDEIVE IETPNGDVKR GQVLESSDGF VAIQVFEGTE
     GVGKDASVRF LGETLKMPVT EDLLGRVLDG SGNPIDGGPD IVPDDRVDIV GEAINPHARE
     YPEEFIQTGV SGIDGMNTLV RGQKLPIFSG SGLPHSDLAL QIARQASVPE EEAETDDDEG
     SEFAVVFGAM GITAEEANEF MDDFERTGAL ERSVVFMNLA DDPAVERTVT PRMALTTAEY
     LAFEKDYHVL VILTDMTNYC EALRQIGAAR EEVPGRRGYP GYMYTDLAQL YERAGRIEGK
     EGSVTQIPIL TMPGDDDTHP IPDLTGYITE GQIMMNRDLN SQGVTPPVNV LPSLSRLMDD
     GIGEGLTRAD HGDVSDQLYA AYAEGEELRD LVNIVGREAL SERDNRYLDF ADRFEAEFID
     QGFKTNRDIE ETLDLGWELL SMFPKTELNR VDEDLIEDHY VEDVADEATA D