ID   MTRE_META3              Reviewed;         300 AA.
AC   A6UWH3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=Maeo_1269;
OS   Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 /
OS   Nankai-3).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=419665;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA   Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus aeolicus Nankai-3.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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   -!- PATHWAY: One-carbon metabolism; methanogenesis from CO(2); methyl-
CC       coenzyme M from 5,10-methylene-5,6,7,8-tetrahydromethanopterin: step
CC       2/2. {ECO:0000255|HAMAP-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; CP000743; ABR56845.1; -; Genomic_DNA.
DR   RefSeq; WP_011973977.1; NC_009635.1.
DR   AlphaFoldDB; A6UWH3; -.
DR   STRING; 419665.Maeo_1269; -.
DR   EnsemblBacteria; ABR56845; ABR56845; Maeo_1269.
DR   GeneID; 5326487; -.
DR   KEGG; mae:Maeo_1269; -.
DR   eggNOG; arCOG04870; Archaea.
DR   HOGENOM; CLU_958513_0_0_2; -.
DR   OMA; QMGNIHR; -.
DR   OrthoDB; 50292at2157; -.
DR   UniPathway; UPA00640; UER00698.
DR   Proteomes; UP000001106; 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:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniPathway.
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; Methanogenesis; Methyltransferase;
KW   One-carbon metabolism; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..300
FT                   /note="Tetrahydromethanopterin S-methyltransferase subunit
FT                   E"
FT                   /id="PRO_1000064942"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01098"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01098"
FT   TRANSMEM        135..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01098"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01098"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01098"
FT   TRANSMEM        261..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01098"
SQ   SEQUENCE   300 AA;  31143 MW;  F73201B082E0FA7B CRC64;
     MDPTLLALGA LALSGAAATV AGCAEDLESD VGSQSNPNSQ VQLGPQMGNI HRYFNKAISG
     EPVSYGLYVA AAGATAWALM GMNLNPILAI IVGSAVAALV HGAYSVSAFL GRIVGQSKNF
     GQPVYMDVMM GHLGPIVGHG FIAVFCMLFA AYLAVNALGN PFPLPLVALI FGITVGAIGS
     STGDVHYGAE REYQKYAFGG GIPVANQGDI DIMAETGIRN GLDSSYFCSK LGGPLTGLAF
     GLIIFLDGWR SILGNIIGGD LITKAAIAIV VGLIVVITTL LLNRKIEVYA RNKFGPYTDR