MTRC_METMA
ID MTRC_METMA Reviewed; 267 AA.
AC O59638;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 26-JUL-2002, sequence version 2.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Tetrahydromethanopterin S-methyltransferase subunit C;
DE EC=2.1.1.86;
DE AltName: Full=N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit C;
GN Name=mtrC; OrderedLocusNames=MM_1545;
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=9559648; DOI=10.1016/s0014-5793(98)00229-4;
RA Lienard T., Gottschalk G.;
RT "Cloning, sequencing and expression of the genes encoding the sodium
RT translocating N5-methyltetrahydromethanopterin:coenzyme M methyltransferase
RT of the methylotrophic archaeon Methanosarcina mazei Go1.";
RL FEBS Lett. 425:204-208(1998).
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: 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.
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;
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.
CC -!- SUBUNIT: The complex is composed of 8 subunits; MtrA, MtrB, MtrC, MtrD,
CC MtrE, MtrF, MtrG and MtrH. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MtrC family. {ECO:0000305}.
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DR EMBL; AF042381; AAC38332.1; -; Genomic_DNA.
DR EMBL; AE008384; AAM31241.1; -; Genomic_DNA.
DR RefSeq; WP_011033491.1; NC_003901.1.
DR AlphaFoldDB; O59638; -.
DR STRING; 192952.MM_1545; -.
DR EnsemblBacteria; AAM31241; AAM31241; MM_1545.
DR GeneID; 44088827; -.
DR GeneID; 66136935; -.
DR KEGG; mma:MM_1545; -.
DR PATRIC; fig|192952.21.peg.1786; -.
DR eggNOG; arCOG04868; Archaea.
DR HOGENOM; CLU_092286_0_0_2; -.
DR OMA; HPFNACL; -.
DR BRENDA; 2.1.1.86; 3270.
DR UniPathway; UPA00640; UER00698.
DR Proteomes; UP000000595; 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..267
FT /note="Tetrahydromethanopterin S-methyltransferase subunit
FT C"
FT /id="PRO_0000147524"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 37..38
FT /note="MP -> NA (in Ref. 1; AAC38332)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="R -> S (in Ref. 1; AAC38332)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 267 AA; 26942 MW; CBD6EE7F2A9B5D45 CRC64;
MSAGGAGGEA KGAYPQQTLM ALGIVGGLVG IYLGHFMPPA YSFFGGIGAI CATVWGADAV
RRVASYGLGT GVPSIGMLAL GMGILAALFG LALGGIAGPI LAVVVAAIIG GVIGALANKV
IGMGIPIMEQ AMIEISCAGT LVILGLSVVI AGSFDYAAII ENVIANGYIA LIFIIGGMGI
LHPFNACLGP DESQDRTLIL AVEKAAIALI ITGFASSLHE GLMTAGINIL VGLVIWYVAF
SKYYALIKRD AYAVVGTGLL PSAEELQ
