ID   VATB_PICTO              Reviewed;         460 AA.
AC   Q6L1S8;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 111.
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=PTO0489;
OS   Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS   100828).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Picrophilaceae; Picrophilus.
OX   NCBI_TaxID=263820;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX   PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA   Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA   Schepers B., Dock C., Antranikian G., Liebl W.;
RT   "Genome sequence of Picrophilus torridus and its implications for life
RT   around pH 0.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
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   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255|HAMAP-Rule:MF_00310}.
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DR   EMBL; AE017261; AAT43074.1; -; Genomic_DNA.
DR   RefSeq; WP_011177290.1; NC_005877.1.
DR   AlphaFoldDB; Q6L1S8; -.
DR   SMR; Q6L1S8; -.
DR   STRING; 263820.PTO0489; -.
DR   EnsemblBacteria; AAT43074; AAT43074; PTO0489.
DR   GeneID; 2845218; -.
DR   KEGG; pto:PTO0489; -.
DR   PATRIC; fig|263820.9.peg.515; -.
DR   eggNOG; arCOG00865; Archaea.
DR   HOGENOM; CLU_022916_0_0_2; -.
DR   OMA; ICELRTP; -.
DR   OrthoDB; 8899at2157; -.
DR   Proteomes; UP000000438; 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   PIRSF; PIRSF039114; V-ATPsynth_beta/V-ATPase_B; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Hydrogen ion transport; Ion transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..460
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_0000144660"
SQ   SEQUENCE   460 AA;  50993 MW;  4B1A1AB78DAD35F3 CRC64;
     MRDVLYRSVS QISGPLLFVE DVKDTSYNEI VDIILDNGEK RRGQVLETRN GLSIVQIYGS
     TTGISTSNAS VKFTGSTFRL PVSDDMLGRI FNGFGEPIDN GPKIYSKDKL DINGSAINPY
     SREEPSEFVQ TGISTIDGMN TLVMGQKLPI FSGAGLSHNR LAAQIARQAK TLKGGENFGV
     VFGAIGITSE EANYFINEFQ SSGSLSNSVI FLNLASDPSM DRIVLPRIAL TTAEYLAYEK
     EMNMLVILTD MTNYCEALRE ISSARNEIPG RRGYPGYMYT DLSTIYERAG KIRGRNGSIT
     QIPILTMPGD DITNPVPDLT GYITEGQITL SRDLNKRNIY PEVDVLLSLS RLMNQGIGSD
     HTREDHRGLA DQLYASYAKG KDARSMSEIV GEESLTETDK LYLKFAEDFE NKYVNQGNIE
     RSIEDTLNLG WDLLSVLPVD EMKKVKSAHI PKYGKWNNGK