ID   MTRA_METST              Reviewed;         249 AA.
AC   Q2NI29;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Tetrahydromethanopterin S-methyltransferase subunit A {ECO:0000255|HAMAP-Rule:MF_01093};
DE            EC=2.1.1.86 {ECO:0000255|HAMAP-Rule:MF_01093};
DE   AltName: Full=N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit A {ECO:0000255|HAMAP-Rule:MF_01093};
GN   Name=mtrA {ECO:0000255|HAMAP-Rule:MF_01093}; OrderedLocusNames=Msp_0304;
OS   Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS   MCB-3).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX   NCBI_TaxID=339860;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX   PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA   Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA   Gottschalk G., Thauer R.K.;
RT   "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT   intestinal archaeon is restricted to methanol and H2 for methane formation
RT   and ATP synthesis.";
RL   J. Bacteriol. 188:642-658(2006).
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_01093}.
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_01093};
CC   -!- COFACTOR:
CC       Name=5-hydroxybenzimidazolylcob(I)amide; Xref=ChEBI:CHEBI:60494;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01093};
CC       Note=Binds 1 5-hydroxybenzimidazolylcobamide group. {ECO:0000255|HAMAP-
CC       Rule:MF_01093};
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_01093}.
CC   -!- SUBUNIT: The complex is composed of 8 subunits; MtrA, MtrB, MtrC, MtrD,
CC       MtrE, MtrF, MtrG and MtrH. {ECO:0000255|HAMAP-Rule:MF_01093}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01093};
CC       Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01093}.
CC   -!- SIMILARITY: Belongs to the MtrA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01093}.
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DR   EMBL; CP000102; ABC56714.1; -; Genomic_DNA.
DR   RefSeq; WP_011405914.1; NC_007681.1.
DR   AlphaFoldDB; Q2NI29; -.
DR   SMR; Q2NI29; -.
DR   STRING; 339860.Msp_0304; -.
DR   EnsemblBacteria; ABC56714; ABC56714; Msp_0304.
DR   GeneID; 41324877; -.
DR   KEGG; mst:Msp_0304; -.
DR   eggNOG; arCOG03221; Archaea.
DR   HOGENOM; CLU_100863_0_0_2; -.
DR   OMA; ARMKIVS; -.
DR   OrthoDB; 89197at2157; -.
DR   UniPathway; UPA00640; UER00698.
DR   Proteomes; UP000001931; Chromosome.
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:0050897; F:cobalt ion binding; 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_01093; MtrA; 1.
DR   InterPro; IPR030688; MeTrfase_MtrA/MtxA.
DR   InterPro; IPR005778; MtrA.
DR   Pfam; PF04208; MtrA; 1.
DR   PIRSF; PIRSF500207; MtrA; 1.
DR   PIRSF; PIRSF009452; MtrA_MtxA; 1.
DR   TIGRFAMs; TIGR01111; mtrA; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cobalt; Membrane; Methanogenesis; Methyltransferase;
KW   One-carbon metabolism; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..249
FT                   /note="Tetrahydromethanopterin S-methyltransferase subunit
FT                   A"
FT                   /id="PRO_0000403067"
FT   TOPO_DOM        1..227
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01093"
FT   TRANSMEM        228..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01093"
FT   TOPO_DOM        249
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01093"
FT   BINDING         84
FT                   /ligand="5-hydroxybenzimidazolylcob(I)amide"
FT                   /ligand_id="ChEBI:CHEBI:60494"
FT                   /ligand_note="cofactor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01093"
SQ   SEQUENCE   249 AA;  26969 MW;  CC99C2DC53AA5E1D CRC64;
     MADKKEVIQN WPLETGDYAV GNVESPVAVV SLGSNMNDEL VAAGAAISGP LHTENLGIEK
     VVANIISNSN IRYVLICGSE VQGHITGKTV EALYENGIDE EKKSIIGSPG AIPFVENLPV
     EAVERFQKQV SIVSMINNED VSEISSKIDE CISNDPGAYD EDAMIVEFNE TPEEEFEVDE
     VTFSDDSAVD LASIVLLEVE NRISMMNNEI KQIASLEKIS SGYYAGKIEG IVIGFILTLV
     FLIIIIQGL