ID   VATB_STRGC              Reviewed;         464 AA.
AC   A8AUJ8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=SGO_0136;
OS   Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS   DL1 / V288).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=467705;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX   PubMed=17720781; DOI=10.1128/jb.01023-07;
RA   Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT   "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT   to competence signaling peptide.";
RL   J. Bacteriol. 189:7799-7807(2007).
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; CP000725; ABV09355.1; -; Genomic_DNA.
DR   RefSeq; WP_002902006.1; NC_009785.1.
DR   AlphaFoldDB; A8AUJ8; -.
DR   SMR; A8AUJ8; -.
DR   STRING; 467705.SGO_0136; -.
DR   EnsemblBacteria; ABV09355; ABV09355; SGO_0136.
DR   GeneID; 61535464; -.
DR   KEGG; sgo:SGO_0136; -.
DR   eggNOG; COG1156; Bacteria.
DR   HOGENOM; CLU_022916_0_0_9; -.
DR   OMA; GFKIKPR; -.
DR   Proteomes; UP000001131; 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..464
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_1000079068"
SQ   SEQUENCE   464 AA;  51746 MW;  BD31A1D34EFE1A1F CRC64;
     MSVIKEYRTV SEVVGPLMIV DQVAGVHFNE LVEIQLHDGS KRQGQVLEVQ EDKAMVQLFE
     GSSGINLEKA KVRFTGRPLE LPVSEDMVGR IFNGMGKPID GGPAILPEKY LDIDGQAINP
     VARDYPDEFI QTGISAIDHL NTLVRGQKLP VFSGSGLPHK ELAAQIARQA TVLNSDENFA
     VVFAAMGITF EEAEFFMNDL RETGAIDRSV LFINLANDPA IERIATPRIA LTAAEYLAYE
     KDMHVLVIMT DMTNYCEALR EVSAARREVP GRRGYPGYLY TNLSTLYERA GRLVGKKGSV
     TQIPILSMPE DDITHPIPDL TGYITEGQII LSRDLYNSGY RPPINVLPSL SRLKDKGSGE
     GKTRGDHAAT MNQLFAAYAQ GKQAKELAVV LGESALSETD KLYVRFTDRF EQEYINQGFQ
     TNRTIEESLD LGWELLSILP RTELKRIKDD MIDQYLPQTK EEER