ID   VATB_THEPD              Reviewed;         460 AA.
AC   A1RX20;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 79.
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=Tpen_0341;
OS   Thermofilum pendens (strain DSM 2475 / Hrk 5).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermofilales; Thermofilaceae;
OC   Thermofilum.
OX   NCBI_TaxID=368408;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2475 / Hrk 5;
RX   PubMed=18263724; DOI=10.1128/jb.01949-07;
RA   Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E.,
RA   Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M.,
RA   Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B.,
RA   Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.;
RT   "Genome sequence of Thermofilum pendens reveals an exceptional loss of
RT   biosynthetic pathways without genome reduction.";
RL   J. Bacteriol. 190:2957-2965(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   -!- SEQUENCE CAUTION:
CC       Sequence=ABL77750.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000505; ABL77750.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_052885375.1; NC_008698.1.
DR   AlphaFoldDB; A1RX20; -.
DR   SMR; A1RX20; -.
DR   STRING; 368408.Tpen_0341; -.
DR   EnsemblBacteria; ABL77750; ABL77750; Tpen_0341.
DR   GeneID; 4601451; -.
DR   KEGG; tpe:Tpen_0341; -.
DR   eggNOG; arCOG00865; Archaea.
DR   HOGENOM; CLU_022916_0_0_2; -.
DR   OrthoDB; 8899at2157; -.
DR   Proteomes; UP000000641; 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; IPR020003; ATPase_a/bsu_AS.
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.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 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_0000322508"
SQ   SEQUENCE   460 AA;  51612 MW;  D379736D626E3BFB CRC64;
     MYPGKVYRGV KEIRGSLLIV DGIEEAAYDE VVKIYGKDSR ERFGRVLETS IGQAVVQVLG
     DREGLETDTL LKFTGSTFKI RVSEDVIGRV FNGRFEPIDG LPPILSGELR EITGEPINPI
     SREYPHDFIQ TGVSAIDGLF SMVRGQKLPI FSVSGLPHNL LAAQVARQAT VRGEGEQFAV
     VFAGIGLRKT EAEFFLEQFR ETGAIERLVA VLNMADDPAV ERLMTPRIAL TVAEYLAFDL
     DMHVLVIMSD MTNYCEALRE VSSARGEIPG RLGYPGYMYS DLATIYERAG VIKGKKGSIT
     LFPILTMPGG DLRHPIPDLT GYITEGQIFL SQEMYAQGIY PPINILPSLS RLMKSGIGPG
     KTREDHRYLA DQLYDAYSRG VKARDLARII GEIGLSERNR RFLKFAEEFE NKFVNQGFYE
     NRSIEETLDL GWQVLSILPE EELVRIPQKI IEKYHPKYRS