ID   VATB_CLOBA              Reviewed;         459 AA.
AC   B2UWY3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=CLH_2588;
OS   Clostridium botulinum (strain Alaska E43 / Type E3).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=508767;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Alaska E43 / Type E3;
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 genome sequence of Clostridium botulinum E3 str. Alaska E43.";
RL   Submitted (MAY-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001078; ACD52032.1; -; Genomic_DNA.
DR   RefSeq; WP_003370262.1; NC_010723.1.
DR   AlphaFoldDB; B2UWY3; -.
DR   SMR; B2UWY3; -.
DR   KEGG; cbt:CLH_2588; -.
DR   HOGENOM; CLU_022916_0_0_9; -.
DR   OMA; GFKIKPR; -.
DR   OrthoDB; 875807at2; -.
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_1000115654"
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