ID   VATB_PYRCJ              Reviewed;         467 AA.
AC   A3MU07;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=Pcal_0698;
OS   Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=410359;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21063 / JCM 11548 / VA1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA   Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT   "Complete sequence of Pyrobaculum calidifontis JCM 11548.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP000561; ABO08124.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3MU07; -.
DR   SMR; A3MU07; -.
DR   STRING; 410359.Pcal_0698; -.
DR   EnsemblBacteria; ABO08124; ABO08124; Pcal_0698.
DR   KEGG; pcl:Pcal_0698; -.
DR   eggNOG; arCOG00865; Archaea.
DR   HOGENOM; CLU_022916_0_0_2; -.
DR   OMA; MLMMDSV; -.
DR   Proteomes; UP000001431; 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:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00310; ATP_synth_B_arch; 1.
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   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Hydrogen ion transport; Ion transport; Transport.
FT   CHAIN           1..467
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_1000059388"
FT   REGION          95..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   467 AA;  51973 MW;  ADDDA124CB76923C CRC64;
     MLTPVVSYST VREVKGPLLV IERTRGVSYG EIGEVVGPDG EPRKVQVIEV ATDYAVAQVL
     GGTLGLPSKG STVRFYGKTL KIPVSEQLIG RILDGKGQPR DHMPLPPPED FRDVNGEPLN
     PYSREYPEEP IETGISAIDG LYTLVRGQKL PIFSGTGLPH NMMAAQVVRQ STVRGSGEEF
     AVVFVGIGIK TEEALFFMDE FRKTGALRRA VAVINLASDP VAERILAPRV GLTIAEYLAW
     QLGYHVLVVM TDMTNYCEGL RELSSGKGEL PGRRGYPGYM YTDLATIYER AGKAHGKKGS
     VTQFPILTMP NDDITHPIPD LTGYITEGQL VLSRAMWGKG IYPPFDVIMS LSRLAKDAIG
     EGKTREDHKD VANTLIAAYS KALELRNLAT LVGERNLGWR ERRYLRFADA FEQKFIKQGY
     YERRSFEETL DIGWDVLSIL PEDELTNARP QITQKFYRRH IFESVAV