ID   MTRC_METMP              Reviewed;         262 AA.
AC   Q6LWZ2;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Tetrahydromethanopterin S-methyltransferase subunit C {ECO:0000255|HAMAP-Rule:MF_01096};
DE            EC=2.1.1.86 {ECO:0000255|HAMAP-Rule:MF_01096};
DE   AltName: Full=N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit C {ECO:0000255|HAMAP-Rule:MF_01096};
GN   Name=mtrC {ECO:0000255|HAMAP-Rule:MF_01096}; OrderedLocusNames=MMP1562;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
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_01096}.
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_01096};
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_01096}.
CC   -!- SUBUNIT: The complex is composed of 8 subunits; MtrA, MtrB, MtrC, MtrD,
CC       MtrE, MtrF, MtrG and MtrH. {ECO:0000255|HAMAP-Rule:MF_01096}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01096};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01096}.
CC   -!- SIMILARITY: Belongs to the MtrC family. {ECO:0000255|HAMAP-
CC       Rule:MF_01096}.
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DR   EMBL; BX950229; CAF31118.1; -; Genomic_DNA.
DR   RefSeq; WP_011171506.1; NC_005791.1.
DR   AlphaFoldDB; Q6LWZ2; -.
DR   STRING; 267377.MMP1562; -.
DR   EnsemblBacteria; CAF31118; CAF31118; MMP1562.
DR   GeneID; 37876166; -.
DR   KEGG; mmp:MMP1562; -.
DR   PATRIC; fig|267377.15.peg.1600; -.
DR   eggNOG; arCOG04868; Archaea.
DR   HOGENOM; CLU_092286_0_0_2; -.
DR   OMA; HPFNACL; -.
DR   OrthoDB; 61293at2157; -.
DR   BioCyc; MMAR267377:MMP_RS08040-MON; -.
DR   UniPathway; UPA00640; UER00698.
DR   Proteomes; UP000000590; 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: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   HAMAP; MF_01096; MtrC; 1.
DR   InterPro; IPR005865; THM_MeTrfase_su_C.
DR   Pfam; PF04211; MtrC; 1.
DR   PIRSF; PIRSF006530; MtrC; 1.
DR   TIGRFAMs; TIGR01148; mtrC; 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..262
FT                   /note="Tetrahydromethanopterin S-methyltransferase subunit
FT                   C"
FT                   /id="PRO_0000147525"
FT   TRANSMEM        35..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01096"
FT   TRANSMEM        70..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01096"
FT   TRANSMEM        97..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01096"
FT   TRANSMEM        140..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01096"
FT   TRANSMEM        172..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01096"
FT   TRANSMEM        214..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01096"
SQ   SEQUENCE   262 AA;  26607 MW;  FEF9F86305305961 CRC64;
     MSHGGGGHAA ELFPEDQVLA IGAVLSIIGM YVAQFVPSLA MLIGGLLAAG ACVAGANTTR
     RVAAYGLGTG VPSIGMVSLG MGTISALAGV LIPSAFGLPV LATPILAAVI AVVVGFIVGK
     LTQNPVGMKV PIIVSSMTKL SLMGALAILG FCTAFAGGFS ADLIINGAIN NGVIALAFIA
     AGMSILHPFN ACIGPDESHK RTITLAVACG LMAWLIFSIA KLDIVSIVVA AIFWLYTYGS
     FVKMSLGDAC EVKYVPELPK KE