ID   MTRE_METBU              Reviewed;         301 AA.
AC   Q12VU4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Tetrahydromethanopterin S-methyltransferase subunit E {ECO:0000255|HAMAP-Rule:MF_01098};
DE            EC=2.1.1.86 {ECO:0000255|HAMAP-Rule:MF_01098};
DE   AltName: Full=N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit E {ECO:0000255|HAMAP-Rule:MF_01098};
GN   Name=mtrE {ECO:0000255|HAMAP-Rule:MF_01098}; OrderedLocusNames=Mbur_1525;
OS   Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS   ACE-M).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX   NCBI_TaxID=259564;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX   PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA   Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA   De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA   Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA   Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA   Cavicchioli R.;
RT   "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT   burtonii: the role of genome evolution in cold adaptation.";
RL   ISME J. 3:1012-1035(2009).
CC   -!- FUNCTION: Part of a complex that catalyzes the formation of methyl-
CC       coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-
CC       tetrahydromethanopterin. This is an energy-conserving, sodium-ion
CC       translocating step. {ECO:0000255|HAMAP-Rule:MF_01098}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M + 2
CC         Na(+)(in) = 5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M + 2
CC         Na(+)(out); Xref=Rhea:RHEA:53492, ChEBI:CHEBI:29101,
CC         ChEBI:CHEBI:58103, ChEBI:CHEBI:58116, ChEBI:CHEBI:58286,
CC         ChEBI:CHEBI:58319; EC=2.1.1.86; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01098};
CC   -!- SUBUNIT: The complex is composed of 8 subunits; MtrA, MtrB, MtrC, MtrD,
CC       MtrE, MtrF, MtrG and MtrH. {ECO:0000255|HAMAP-Rule:MF_01098}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01098};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01098}.
CC   -!- SIMILARITY: Belongs to the MtrE family. {ECO:0000255|HAMAP-
CC       Rule:MF_01098}.
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DR   EMBL; CP000300; ABE52432.1; -; Genomic_DNA.
DR   RefSeq; WP_011499576.1; NC_007955.1.
DR   AlphaFoldDB; Q12VU4; -.
DR   STRING; 259564.Mbur_1525; -.
DR   EnsemblBacteria; ABE52432; ABE52432; Mbur_1525.
DR   GeneID; 3997348; -.
DR   KEGG; mbu:Mbur_1525; -.
DR   HOGENOM; CLU_958513_0_0_2; -.
DR   OMA; QMGNIHR; -.
DR   OrthoDB; 50292at2157; -.
DR   Proteomes; UP000001979; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0012506; C:vesicle membrane; IEA:InterPro.
DR   GO; GO:0030269; F:tetrahydromethanopterin S-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006814; P:sodium ion transport; IEA:InterPro.
DR   HAMAP; MF_01098; MtrE; 1.
DR   InterPro; IPR005780; MeTrfase_E.
DR   Pfam; PF04206; MtrE; 1.
DR   PIRSF; PIRSF016509; MtrE; 1.
DR   TIGRFAMs; TIGR01113; mtrE; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Methyltransferase; One-carbon metabolism;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..301
FT                   /note="Tetrahydromethanopterin S-methyltransferase subunit
FT                   E"
FT                   /id="PRO_1000064943"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01098"
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01098"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01098"
FT   TRANSMEM        232..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01098"
FT   TRANSMEM        258..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01098"
SQ   SEQUENCE   301 AA;  31934 MW;  E88BD4537D22C5C5 CRC64;
     MEPLMGMGVL ALMGAAATIA GTTEDLESDV GSQSNPNSQV QLAPQMMYPH RIYNKAISGE
     PPSNALICAI GGTVASVLMT ANLSVIFAIA IGALVASAVH GTYCITAYMG RTASQKRFRQ
     PIYLDILRSH TPVMMGYAFI TTFCILVVSY IMVAVLAHPF PLTLLAFIWG ITVGAIGSST
     GDVHYGAERE FQNVEFGSGL NAANSGNIVR KAESGLRNGI DNSWFCAKFG GPVTGLAFGM
     TVFLSGWVTA VFNPAISLTM GWLSVAAGVI LVLLLIIWNR KIEVAARKAF GPYKEEEEVA
     A