ID   VATB1_CLOTE             Reviewed;         461 AA.
AC   Q896K3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=V-type ATP synthase beta chain 1 {ECO:0000255|HAMAP-Rule:MF_00310};
DE   AltName: Full=V-ATPase subunit B 1 {ECO:0000255|HAMAP-Rule:MF_00310};
GN   Name=atpB1 {ECO:0000255|HAMAP-Rule:MF_00310}; OrderedLocusNames=CTC_01000;
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88;
RX   PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA   Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA   Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT   disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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; AE015927; AAO35587.1; -; Genomic_DNA.
DR   RefSeq; WP_011099249.1; NC_004557.1.
DR   AlphaFoldDB; Q896K3; -.
DR   SMR; Q896K3; -.
DR   STRING; 212717.CTC_01000; -.
DR   PRIDE; Q896K3; -.
DR   EnsemblBacteria; AAO35587; AAO35587; CTC_01000.
DR   GeneID; 64178765; -.
DR   KEGG; ctc:CTC_01000; -.
DR   HOGENOM; CLU_022916_0_0_9; -.
DR   OMA; GFKIKPR; -.
DR   OrthoDB; 875807at2; -.
DR   Proteomes; UP000001412; 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..461
FT                   /note="V-type ATP synthase beta chain 1"
FT                   /id="PRO_0000322494"
SQ   SEQUENCE   461 AA;  51214 MW;  96B635A8BEEE67F7 CRC64;
     MLKEYRTVKE VVGPLMLVDG VENVKFDELV EIEIQTGEIR RGRVLEINED KALVQLFEGS
     AGINIKGSKA KFLGKPLEIS VSEDMLGRVF DGLGRPKDEG PRIIPEKRLD INGIPINPVA
     RNYPSEFIQT GISAIDGLNT LVRGQKLPVF SGSGLPHAQL AAQIARQAKV LNSDSKFAVV
     FAAVGITFEE AEFFVDDFTK TGAIDRSVLF MNLANDPAIE RIATPRMALT TAEYLAFEKG
     MHVLVILTDL TNYCEALREV SAARKEVPGR RGYPGYLYTD LATLYERAGR IKGKEGSITQ
     IPILTMPEDD KTHPIPDLTG YITEGQIILS RELYRKGVMP PIDVLPSLSR LKDKGIGEGK
     TREDHADTMN QLFAGYAQGK EAKELAVILG ESALSDVDKQ YAKFGDAFEK QYVSQGFTTN
     RTIEETLNLG WELLSILPRT ELKRIRDAYL EKYLPKEKSK E