ID   VATB_BORAP              Reviewed;         434 AA.
AC   Q0SP71; G0IQT8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 102.
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};
GN   OrderedLocusNames=BAPKO_0094, BafPKo_0091;
OS   Borreliella afzelii (strain PKo) (Borrelia afzelii).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=390236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA   Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J.,
RA   Wilske B., Platzer M.;
RT   "Comparative genome analysis: selection pressure on the Borrelia vls
RT   cassettes is essential for infectivity.";
RL   BMC Genomics 7:211-211(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=22123755; DOI=10.1128/jb.05951-11;
RA   Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J.,
RA   Fraser-Liggett C.M., Schutzer S.E.;
RT   "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT   Lyme disease agent isolates.";
RL   J. Bacteriol. 193:6995-6996(2011).
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; CP000395; ABH01357.1; -; Genomic_DNA.
DR   EMBL; CP002933; AEL69324.1; -; Genomic_DNA.
DR   RefSeq; WP_004790416.1; NC_017238.1.
DR   AlphaFoldDB; Q0SP71; -.
DR   SMR; Q0SP71; -.
DR   STRING; 390236.BafPKo_0091; -.
DR   EnsemblBacteria; AEL69324; AEL69324; BafPKo_0091.
DR   KEGG; baf:BAPKO_0094; -.
DR   KEGG; bafz:BafPKo_0091; -.
DR   PATRIC; fig|390236.22.peg.90; -.
DR   eggNOG; COG1156; Bacteria.
DR   HOGENOM; CLU_022916_2_0_12; -.
DR   OMA; GFKIKPR; -.
DR   OrthoDB; 875807at2; -.
DR   Proteomes; UP000005216; 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; Transport.
FT   CHAIN           1..434
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_1000059365"
SQ   SEQUENCE   434 AA;  48069 MW;  8B7B38F0299C7270 CRC64;
     MKRVYSKIES IAGNVITVTA QGIKYGELAI VKAKDTSSLA EVIKLDREKV SLQVYGGTRG
     VSTSDEIKFL GHTMQVSFSD NLLGRIFDGS GNPRDGGPSL DDNLIEIGGP SANPTKRIVP
     RNMIRTGLPM IDVFNTLVES QKLPIFSVSG EPYNELLVRI ALQAEVDLII LGGMGLKHDD
     YLTFKDSLEK GGALSRTIFF VHTANDSVVE SLTVPDISLS VAEKFALKGK KVLVLLTDMT
     NFADAMKEIS ITMEQVPSNR GYPGDLYSQL AYRYEKAIDF EGAGSITILA VTTMPGDDVT
     HPVPDNTGYI TEGQYYLKGG RIEPFGSLSR LKQMVNSKTR DDHRTIMDTM IKLYASSKES
     VEKKAMGFNM TKWDEKLLKY SNMFESKMMD LSVNIPLEEA LDLGWDILAS CFSPKETGIK
     TDLIQKYWPK KETY