ID   VATB_CLOBJ              Reviewed;         461 AA.
AC   C1FTN6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=CLM_2988;
OS   Clostridium botulinum (strain Kyoto / Type A2).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=536232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kyoto / Type A2;
RA   Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C.,
RA   Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.;
RT   "Genome sequence of Clostridium botulinum A2 Kyoto.";
RL   Submitted (OCT-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; CP001581; ACO86573.1; -; Genomic_DNA.
DR   RefSeq; WP_012705391.1; NC_012563.1.
DR   AlphaFoldDB; C1FTN6; -.
DR   SMR; C1FTN6; -.
DR   STRING; 536232.CLM_2988; -.
DR   EnsemblBacteria; ACO86573; ACO86573; CLM_2988.
DR   KEGG; cby:CLM_2988; -.
DR   eggNOG; COG1156; Bacteria.
DR   HOGENOM; CLU_022916_0_0_9; -.
DR   OMA; GFKIKPR; -.
DR   Proteomes; UP000001374; 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; Transport.
FT   CHAIN           1..461
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_1000132887"
SQ   SEQUENCE   461 AA;  51135 MW;  1C9018C8DA4EBA54 CRC64;
     MLKEYRTVKE VVGPLMLVDQ VESVSFDELV EIELHNGEKR RGRVLEINKD KALVQLFEGS
     AGINIKGAKV KFLGKPLELG VSEDMLGRVF DGLGNPKDGG PKIIADEKRD ISGIPINPVA
     RNYPDEFIQT GVSAIDGLNT LVRGQKLPVF SGSGLPHAEL AAQIARQAKV LKSDSKFAVV
     FAAIGTTFEE AQYFIDDFTK TGAIDRAVLF INLANDPAIE RIATPRMALT AAEYLAFEKG
     MHVLVIMTDI TNYCEALREV SAARKEVPGR RGYPGYLYTD LSTIYERAGR ILGKEGSITQ
     IPILTMPEDD KTHPIPDLTG YITEGQIILS RELYKKGIMP PIDVLPSLSR LKDKGIGKEK
     TREDHADTMN QLFAAYAQGK QAKELSVILG ESALSDTDKL YAKFADAFEE EYVSQGFTTN
     RTIEETLNLG WKLLTILPKS ELKRIRDEYL EKYLNKAEES K