ID   VATB_CLOBB              Reviewed;         459 AA.
AC   B2TP90;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
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=CLL_A2860;
OS   Clostridium botulinum (strain Eklund 17B / Type B).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=935198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Eklund 17B / Type B;
RA   Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Complete sequence of Clostridium botulinum strain Eklund.";
RL   Submitted (APR-2008) 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; CP001056; ACD22914.1; -; Genomic_DNA.
DR   RefSeq; WP_003370262.1; NC_018648.1.
DR   AlphaFoldDB; B2TP90; -.
DR   SMR; B2TP90; -.
DR   EnsemblBacteria; ACD22914; ACD22914; CLL_A2860.
DR   KEGG; cbk:CLL_A2860; -.
DR   PATRIC; fig|935198.13.peg.2821; -.
DR   HOGENOM; CLU_022916_0_0_9; -.
DR   OMA; GFKIKPR; -.
DR   OrthoDB; 875807at2; -.
DR   Proteomes; UP000001195; Chromosome.
DR   GO; GO:0045259; C:proton-transporting ATP synthase complex; IEA:UniProt.
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; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
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; SSF50615; SSF50615; 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; Transport.
FT   CHAIN           1..459
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_1000115655"
SQ   SEQUENCE   459 AA;  51082 MW;  85433C51E50AF261 CRC64;
     MLKEYRTVTE VVGPLMVVEG VEGVKYDELV EIELHTGEKR RGKVLEVNGS KAMVQIFEGS
     SGINLKGTKA KFLGRPLELG VSEDMLGRVF DGMGRPNDNG PDIIPEKRVD INGEAINPMA
     RDFPSEFIQT GVSAIDGLNT LVRGQKLPVF SAAGLPHAEL AAQIARQAKV LNSDSKFAIV
     FAAIGITFEE AQFFQDEFKR TGAIDRSVLF MNLASDPAIE RIATPRMALT CAEYLAYEKG
     MQVLVIMTDI TNYAEALREI SAARKEVPGR RGYPGYLYTD LSTLYERAGR LRGKEGSITQ
     IPILTMPEDD KTHPIPDLTG YITEGQIILS RELYKKGIMP PIDVLPSLSR LKDKGIGKGK
     TREDHADTMN QLFAAYSQGK QAKELSAILG ESALSDTDKK LAKFAEAFED EYVSQGFNTN
     RTIEETLNLG WKLLKMLPRT ELKRIRDEYL EKYMPREEE