ID   VATE_METMA              Reviewed;         183 AA.
AC   Q60183;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   26-JUL-2002, sequence version 2.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=V-type ATP synthase subunit E;
DE   AltName: Full=V-ATPase subunit E;
GN   Name=atpE; Synonyms=ahaE; OrderedLocusNames=MM_0783;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=8702544; DOI=10.1074/jbc.271.31.18843;
RA   Wilms R., Freiberg C., Wegerle E., Meier I., Mayer F., Mueller V.;
RT   "Subunit structure and organization of the genes of the A1A0 ATPase from
RT   the Archaeon Methanosarcina mazei Go1.";
RL   J. Biol. Chem. 271:18843-18852(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane.
CC   -!- SUBUNIT: Composed of seven subunits; A, B, C, D, E, F and G.
CC   -!- SIMILARITY: Belongs to the V-ATPase E subunit family. {ECO:0000305}.
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DR   EMBL; U47274; AAC06372.1; -; Genomic_DNA.
DR   EMBL; AE008384; AAM30479.1; -; Genomic_DNA.
DR   PIR; T45104; T45104.
DR   RefSeq; WP_011032733.1; NC_003901.1.
DR   AlphaFoldDB; Q60183; -.
DR   SMR; Q60183; -.
DR   STRING; 192952.MM_0783; -.
DR   TCDB; 3.A.2.3.1; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR   EnsemblBacteria; AAM30479; AAM30479; MM_0783.
DR   GeneID; 24876678; -.
DR   GeneID; 66137820; -.
DR   KEGG; mma:MM_0783; -.
DR   PATRIC; fig|192952.21.peg.931; -.
DR   eggNOG; arCOG00869; Archaea.
DR   HOGENOM; CLU_120786_0_0_2; -.
DR   OMA; YAGNIDC; -.
DR   Proteomes; UP000000595; 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.
DR   Pfam; PF01991; vATP-synt_E; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Hydrogen ion transport; Ion transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..183
FT                   /note="V-type ATP synthase subunit E"
FT                   /id="PRO_0000117318"
FT   CONFLICT        3
FT                   /note="L -> H (in Ref. 1; AAC06372)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        97
FT                   /note="P -> S (in Ref. 1; AAC06372)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   183 AA;  20386 MW;  63C59C4EBBC3EDB8 CRC64;
     MGLEIVVKDI QEGARAEVSR IKAEGDAKAS EIINEAKEIQ KKTLGDSLAK AEEDLQSLHQ
     QVISSANLEV KRITLNKRKE LLDTVYNQTV ENIKSMPASK KEELLKSILD KHEASGARAY
     SSKESEELVK KLTSLSYAGN IDSIGGIVLE NEDRTVRLDF TYDSILKSVY ERSLKQISDI
     LYG