ID   VATB_STRPQ              Reviewed;         471 AA.
AC   P0DA09; Q79YM9; Q7CFI7;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 59.
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=SPs0123;
OS   Streptococcus pyogenes serotype M3 (strain SSI-1).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=193567;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSI-1;
RX   PubMed=12799345; DOI=10.1101/gr.1096703;
RA   Nakagawa I., Kurokawa K., Yamashita A., Nakata M., Tomiyasu Y.,
RA   Okahashi N., Kawabata S., Yamazaki K., Shiba T., Yasunaga T., Hayashi H.,
RA   Hattori M., Hamada S.;
RT   "Genome sequence of an M3 strain of Streptococcus pyogenes reveals a large-
RT   scale genomic rearrangement in invasive strains and new insights into phage
RT   evolution.";
RL   Genome Res. 13:1042-1055(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; BA000034; BAC63218.1; -; Genomic_DNA.
DR   RefSeq; WP_002986419.1; NC_004606.1.
DR   AlphaFoldDB; P0DA09; -.
DR   SMR; P0DA09; -.
DR   GeneID; 57851988; -.
DR   KEGG; sps:SPs0123; -.
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..471
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_0000411286"
SQ   SEQUENCE   471 AA;  52358 MW;  F12477A7A2FB1728 CRC64;
     MSVLKEYRTV SEVVGPLMIV DQVAGVHYNE LVDITLHNGE RRKGQVLEVQ GDKAMVQLFE
     GSTGINLAKT KVRFTGHPLE LAVSEDMVGR IFDGMGQPID GGPELIPEKY LDIDGQAINP
     VARDYPDEFI QTGISAIDHL NTLVRGQKLP VFSGSGLPHN ELAAQIARQA TVLNSDDNFA
     VVFAAMGITF EEAEFFMNDL RETGAIDRSV LFINLANDPA IERIATPRIA LTTAEYLAYE
     KGMHVLVIMT DMTNYCEALR EVSAARREVP GRRGYPGYLY TNLSTLYERA GRLIGKKGSV
     TQIPILTMPE DDITHPIPDL TGYITEGQII LSQELYKNGF RPPINVLPSL SRLKDKGSGE
     GKTRQDHAAT MNQLFAAYAQ GKQAKELAVV LGESALSETD KLYVAFTNRF EEEYINQGFY
     TNRSIEESLD LGWELLSILP RTELKRIKDD MLDRYLPKAD TTMTKVFVAN D