ID   VATE_BORAP              Reviewed;         199 AA.
AC   Q0SP68; G0IQU1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=V-type ATP synthase subunit E;
DE   AltName: Full=V-ATPase subunit E {ECO:0000255|HAMAP-Rule:MF_00311};
GN   Name=atpE {ECO:0000255|HAMAP-Rule:MF_00311};
GN   OrderedLocusNames=BAPKO_0097, BafPKo_0094;
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. {ECO:0000255|HAMAP-Rule:MF_00311}.
CC   -!- SIMILARITY: Belongs to the V-ATPase E subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_00311}.
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DR   EMBL; CP000395; ABH01360.1; -; Genomic_DNA.
DR   EMBL; CP002933; AEL69327.1; -; Genomic_DNA.
DR   RefSeq; WP_004790537.1; NC_017238.1.
DR   AlphaFoldDB; Q0SP68; -.
DR   SMR; Q0SP68; -.
DR   STRING; 390236.BafPKo_0094; -.
DR   EnsemblBacteria; AEL69327; AEL69327; BafPKo_0094.
DR   KEGG; baf:BAPKO_0097; -.
DR   KEGG; bafz:BafPKo_0094; -.
DR   PATRIC; fig|390236.22.peg.93; -.
DR   eggNOG; COG1390; Bacteria.
DR   HOGENOM; CLU_105793_0_1_12; -.
DR   OMA; MQFEVKD; -.
DR   OrthoDB; 1478141at2; -.
DR   Proteomes; UP000005216; Chromosome.
DR   GO; GO:0033178; C:proton-transporting two-sector ATPase complex, catalytic domain; IEA:InterPro.
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:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00311; ATP_synth_E_arch; 1.
DR   InterPro; IPR002842; ATPase_V1_Esu.
PE   3: Inferred from homology;
KW   ATP synthesis; Hydrogen ion transport; Ion transport; Transport.
FT   CHAIN           1..199
FT                   /note="V-type ATP synthase subunit E"
FT                   /id="PRO_0000322509"
SQ   SEQUENCE   199 AA;  22741 MW;  E8B288D7F9619AE2 CRC64;
     MQFEVKDLIN KIKKDGLEEA ERVSNDIILK AKREAEEIVA RAEESARALK AKSEKEINDY
     KSHALEASRQ AIRDLIIGVE KNLKSLFENT LKDNVVEVFS DNNFLAELII KITDSWAKEE
     KLVVQLNESD FSSLEQILRL KLGNKLAQGI EIKPFKGISK GFKIQKKNIG LQYDFSAETV
     ADILFDYLNP RFKEIIKVV