MTRF_METMA
ID MTRF_METMA Reviewed; 72 AA.
AC P80654; O59641;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=Tetrahydromethanopterin S-methyltransferase subunit F;
DE EC=2.1.1.86;
DE AltName: Full=N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit F;
GN Name=mtrF; OrderedLocusNames=MM_1542;
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).
RN [3]
RP PROTEIN SEQUENCE OF 2-16.
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=8774736; DOI=10.1111/j.1432-1033.1996.0857u.x;
RA Lienard T., Becher B., Marschall M., Bowien S., Gottschalk G.;
RT "Sodium ion translocation by N5-methyltetrahydromethanopterin: coenzyme M
RT methyltransferase from Methanosarcina mazei Go1 reconstituted in ether
RT lipid liposomes.";
RL Eur. J. Biochem. 239:857-864(1996).
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}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MtrF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM31238.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF042381; AAC38335.1; -; Genomic_DNA.
DR EMBL; AE008384; AAM31238.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_015411901.1; NC_003901.1.
DR AlphaFoldDB; P80654; -.
DR SMR; P80654; -.
DR STRING; 192952.MM_1542; -.
DR EnsemblBacteria; AAM31238; AAM31238; MM_1542.
DR GeneID; 1479884; -.
DR GeneID; 24883167; -.
DR GeneID; 44088830; -.
DR GeneID; 66136932; -.
DR KEGG; mma:MM_1542; -.
DR PATRIC; fig|192952.21.peg.1783; -.
DR eggNOG; arCOG03381; Archaea.
DR HOGENOM; CLU_188097_0_0_2; -.
DR OMA; PQMGAID; -.
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_01099; MtrF; 1.
DR InterPro; IPR011307; MeTrfase_F.
DR InterPro; IPR013347; MeTrfase_F_su.
DR Pfam; PF09472; MtrF; 1.
DR PIRSF; PIRSF006523; MtrF; 1.
DR TIGRFAMs; TIGR02507; MtrF; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Membrane; Methanogenesis;
KW Methyltransferase; One-carbon metabolism; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8774736"
FT CHAIN 2..72
FT /note="Tetrahydromethanopterin S-methyltransferase subunit
FT F"
FT /id="PRO_0000147550"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 42
FT /note="S -> F (in Ref. 1; AAC38335)"
FT /evidence="ECO:0000305"
FT CONFLICT 47..49
FT /note="TGI -> PD (in Ref. 1; AAC38335)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="F -> L (in Ref. 1; AAC38335)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 72 AA; 7568 MW; C41F8A29453BA312 CRC64;
MAEEHEKGVP MVLAPQMGAI DATVESIRYR AQLIARNQKL DSGVAATGII GFAAGFLFSL
LMVIVLPVAV GL
