ID   VATB2_TREPA             Reviewed;         480 AA.
AC   O83540;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=V-type ATP synthase beta chain 2;
DE   AltName: Full=V-ATPase subunit B 2;
GN   Name=atpB2; OrderedLocusNames=TP_0528;
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA   McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA   Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA   Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL   Science 281:375-388(1998).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   EMBL; AE000520; AAC65515.1; -; Genomic_DNA.
DR   PIR; B71313; B71313.
DR   RefSeq; WP_010881976.1; NC_021490.2.
DR   AlphaFoldDB; O83540; -.
DR   SMR; O83540; -.
DR   IntAct; O83540; 7.
DR   STRING; 243276.TPANIC_0528; -.
DR   TCDB; 3.A.2.3.3; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR   EnsemblBacteria; AAC65515; AAC65515; TP_0528.
DR   GeneID; 57879052; -.
DR   KEGG; tpa:TP_0528; -.
DR   eggNOG; COG1156; Bacteria.
DR   HOGENOM; CLU_022916_0_0_12; -.
DR   OMA; ICELRTP; -.
DR   OrthoDB; 875807at2; -.
DR   Proteomes; UP000000811; 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; 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.
PE   3: Inferred from homology;
KW   ATP synthesis; Hydrogen ion transport; Ion transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..480
FT                   /note="V-type ATP synthase beta chain 2"
FT                   /id="PRO_0000144684"
SQ   SEQUENCE   480 AA;  53057 MW;  D02C999311D3EF92 CRC64;
     MKGVWYRGLS SIDGPIVVAK RREGAFYGEI TAIRDRFGAL RTGRIIDLSQ ECCLIQVFGS
     TLGLSLDGAC LEFLDVPMQL RVCEGLMGRV FDGLGRPIDG FPEVLSSQLR NVNGYPINPY
     ARVYPRDFIQ TGISAIDGMN TLIRGQKLPI FSGNGLAHNR LAAQIIRQAK ILGTDEAFVM
     VFAGMGIKHD VARFFVSSFE ETGVLSKVVM FLSLADAPSI ERIITPRCAL TAAEYLAFEK
     NKHVLVIFTD MTNYCEALRE VSTTRGEVPG RKGYPGYLYS DLAELYERAG RVKGSSGSVT
     QIPILTMPND DISHPIPDLT GYITEGQIVL QRDLSQRGLY PPIGCLPSLS RLMKDGIGEG
     MTRADHHAVS SQLFASYARV QSVRSLASIV GEEELPALDK CYLRFGDLFE QYFLTQDEHE
     DRSISQTLDI GWSLLSLLPR TELYRIDPKL IDQYLTASCS AVSDQLRKAI EEARTPVADA