ID   VATB2_CLOTE             Reviewed;         460 AA.
AC   Q891P2;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=V-type ATP synthase beta chain 2 {ECO:0000255|HAMAP-Rule:MF_00310};
DE   AltName: Full=V-ATPase subunit B 2 {ECO:0000255|HAMAP-Rule:MF_00310};
GN   Name=atpB2 {ECO:0000255|HAMAP-Rule:MF_00310}; OrderedLocusNames=CTC_02327;
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}.
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; AE015927; AAO36803.1; -; Genomic_DNA.
DR   RefSeq; WP_011100464.1; NC_004557.1.
DR   AlphaFoldDB; Q891P2; -.
DR   SMR; Q891P2; -.
DR   STRING; 212717.CTC_02327; -.
DR   EnsemblBacteria; AAO36803; AAO36803; CTC_02327.
DR   GeneID; 64179596; -.
DR   KEGG; ctc:CTC_02327; -.
DR   HOGENOM; CLU_022916_0_0_9; -.
DR   OMA; ICELRTP; -.
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   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..460
FT                   /note="V-type ATP synthase beta chain 2"
FT                   /id="PRO_0000322495"
SQ   SEQUENCE   460 AA;  51397 MW;  820DC5348499DE01 CRC64;
     MRKEYLLLDR VQGPLVVLSE VEGVAYDEIV EIKIANGETK KGRVVQLQGD KAVIQVFEST
     TGMSLQNTTI SFTGKPLEIS LSREVLGREF NGIGEAIDGR GEIYSLKKYN VNGRPINPVA
     RKYPRNFIQT GISSIDCLTT LIRGQKLPIF SGNGMPHNEL AAQIIRQAKI GGGDGEEKFA
     VVFAAMGIKH DDKEFFRKKF EEAGVIDRLV MFTNLADDPI VERITTPRAA LTTAEYLAFE
     EGMHILVIMT DITNYCEALR ELSSSREEVP SRKGYPGYLY SDLASLYERA GMMEGKDGSI
     TQLPILTMPN DDITHPIPDL TGYITEGQIV LSRDLSGKNI YPPVNILPSL SRLMKDGIGE
     GYTREDHAEV SNQLFASYSY VQDVISLSQV IGEDELSPVD KIYMEFGREF ESKFLNQGFE
     DNRSIDETLD LAWEILSILP KSQLDRVSPE ALEKHYRGDK