ID   VATB_STRP4              Reviewed;         461 AA.
AC   B5E551;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=SPG_1209;
OS   Streptococcus pneumoniae serotype 19F (strain G54).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=512566;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G54;
RX   PubMed=11442348; DOI=10.1089/10766290152044995;
RA   Dopazo J., Mendoza A., Herrero J., Caldara F., Humbert Y., Friedli L.,
RA   Guerrier M., Grand-Schenk E., Gandin C., de Francesco M., Polissi A.,
RA   Buell G., Feger G., Garcia E., Peitsch M., Garcia-Bustos J.F.;
RT   "Annotated draft genomic sequence from a Streptococcus pneumoniae type 19F
RT   clinical isolate.";
RL   Microb. Drug Resist. 7:99-125(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G54;
RA   Mulas L., Trappetti C., Hakenbeck R., Iannelli F., Pozzi G., Davidsen T.M.,
RA   Tettelin H., Oggioni M.;
RT   "Pneumococcal beta glucoside metabolism investigated by whole genome
RT   comparison.";
RL   Submitted (MAR-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; CP001015; ACF56557.1; -; Genomic_DNA.
DR   RefSeq; WP_000111248.1; NC_011072.1.
DR   AlphaFoldDB; B5E551; -.
DR   SMR; B5E551; -.
DR   GeneID; 61380552; -.
DR   KEGG; spx:SPG_1209; -.
DR   HOGENOM; CLU_022916_0_0_9; -.
DR   OMA; GFKIKPR; -.
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_1000115663"
SQ   SEQUENCE   461 AA;  51595 MW;  2A1C4CFAC6AE6A8C CRC64;
     MSVIKEYRTA SEVVGPLMIV EQVNNVSYNE LVEIQLHNGE IRRGQVLEIH EDKAMVQLFE
     GSSGINLEKS KIRFAGHALE LAVSEDMVGR IFNGMGKPID GGPDLIPEKY LDIDGQAINP
     VSRDYPDEFI QTGISSIDHL NTLVRGQKLP VFSGSGLPHN ELAAQIARQA TVLNSDENFA
     VVFAAMGITF EEAEFFMEEL RKTGAIDRSV LFMNLANDPA IERIATPRIA LTAAEYLAFE
     KDMHVLVIMT DMTNYCEALR EVSAARREVP GRRGYPGYLY TNLSTLYERA GRLVGKKGSV
     TQIPILTMPE DDITHPIPDL TGYITEGQII LSHELYNQGY RPPINVLPSL SRLKDKGSGE
     GKTRGDHAPT MNQLFAAYAQ GKKVEELAVV LGESALSDVD KLYVRFTKRF EEEYINQGFY
     KNRNIEDTLN LGWELLSILP RTELKRIKDD LLDKYLPLVE V