ID   VATB_DEIDV              Reviewed;         471 AA.
AC   C1CXU4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 66.
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=Deide_01000;
OS   Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=546414;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115;
RX   PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA   de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA   Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA   Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT   "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT   bacterium Deinococcus deserti.";
RL   PLoS Genet. 5:E1000434-E1000434(2009).
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; CP001114; ACO44900.1; -; Genomic_DNA.
DR   RefSeq; WP_012692023.1; NC_012526.1.
DR   AlphaFoldDB; C1CXU4; -.
DR   SMR; C1CXU4; -.
DR   STRING; 546414.Deide_01000; -.
DR   PaxDb; C1CXU4; -.
DR   EnsemblBacteria; ACO44900; ACO44900; Deide_01000.
DR   KEGG; ddr:Deide_01000; -.
DR   eggNOG; COG1156; Bacteria.
DR   HOGENOM; CLU_022916_0_0_0; -.
DR   OMA; ICELRTP; -.
DR   OrthoDB; 875807at2; -.
DR   Proteomes; UP000002208; 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..471
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_1000205041"
SQ   SEQUENCE   471 AA;  51388 MW;  97FC5A2571AB0DD1 CRC64;
     MTLLQKEYND VAYISGPLLF VNAASDLAYG AIVNIKDASG RSRGGQVISV TDQNAVIQVF
     EETRGLDLAT ASVSLVEDVA RLGVSKEMIG RRFDGLGRPI DGLPQVVAEQ RLSINGQAMN
     PAARAKPEEF IQTGISTIDV QTSLIRGQKL PIFSGSGLPH NELAAQIARQ AKVPGHEGDF
     AVVFAAMGLT QREVSFFTQE FERTGALARS VLFLNKADDP AVERLLTPRM ALTTAEYLAF
     EHGYHVLVIL TDLTNYCEAL REIGGAREEI PGRRGFPGYM YTDLASLYER AGVVEGKPGS
     VTQVPILSMP DDDITHPIPD LTGYITEGQI VVDRTLNSKG VFPPINPLPS LSRLQGNGIG
     KGKTRADHKN ISDQLFAAYA NGLDLRKLVA ITGEDALTET DKLYLRFADD FEQYFIGQGD
     QDRSIDDSLT VAWGILSKLP QSQLTRISKD AIDKYYGTKM DEMWKGSRSL G