ID   VATB_DEIGD              Reviewed;         470 AA.
AC   Q1IWP4;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=Dgeo_2046;
OS   Deinococcus geothermalis (strain DSM 11300 / AG-3a).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=319795;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11300 / AG-3a;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J.,
RA   Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300.";
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. The V-type 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; CP000359; ABF46340.1; -; Genomic_DNA.
DR   RefSeq; WP_011531166.1; NC_008025.1.
DR   AlphaFoldDB; Q1IWP4; -.
DR   SMR; Q1IWP4; -.
DR   STRING; 319795.Dgeo_2046; -.
DR   EnsemblBacteria; ABF46340; ABF46340; Dgeo_2046.
DR   KEGG; dge:Dgeo_2046; -.
DR   eggNOG; COG1156; Bacteria.
DR   HOGENOM; CLU_022916_0_0_0; -.
DR   OMA; ICELRTP; -.
DR   OrthoDB; 875807at2; -.
DR   Proteomes; UP000002431; 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   PIRSF; PIRSF039114; V-ATPsynth_beta/V-ATPase_B; 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..470
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_0000322497"
SQ   SEQUENCE   470 AA;  51377 MW;  5E02ADA1AB5ED7DC CRC64;
     MTTLLKKEYN DVSYISGPLL FVNAASDLAY GAIVEIKDGT GRTRGGQVIS VSDENAVIQV
     FEETRGLDLA TASVSLVEDV ARLGVSREMI GRRFDGLGRP IDGLPPVVAE KRLNINGEPM
     NPAARAKPEE FIQTGISTID VNTSLIRGQK LPIFSGSGLP HNELAAQIAR QAKVPGHEGD
     FAVVFAAMGL TQREVSFFTQ EFERTGALAR SVLFLNRADD PAVERLLTPR MALTTAEYLA
     FEHGYHVLVI LTDMTNYCEA LREIGGAREE IPGRRGFPGY MYTDLASLYE RAGVVQGKPG
     SVTQIPILSM PDDDITHPIP DLTGYITEGQ IVVDRGLNAK GIFPPINPLP SLSRLQGNGI
     GKGKTRADHK NVSDQLFAAY ANGLDLRKLV AITGEDALTE TDKLYLRFAD DFEAYFIGQG
     DQDRSVEDSL TVAWAILSKL PQSQLTRLSK DAIDKYYGAK LDEMWRGNRI