ID   MTSB_METMA              Reviewed;         275 AA.
AC   Q8PUA7;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Methylated-thiol--corrinoid protein MtsB;
GN   Name=mtsB; OrderedLocusNames=MM_2428;
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 [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: Harbors a corrinoid prosthetic group and acts as a methyl
CC       group carrier in methanogenesis from methylated-thiols. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the methylamine corrinoid protein family.
CC       {ECO:0000305}.
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DR   EMBL; AE008384; AAM32124.1; -; Genomic_DNA.
DR   RefSeq; WP_011034352.1; NC_003901.1.
DR   AlphaFoldDB; Q8PUA7; -.
DR   SMR; Q8PUA7; -.
DR   STRING; 192952.MM_2428; -.
DR   EnsemblBacteria; AAM32124; AAM32124; MM_2428.
DR   GeneID; 44087801; -.
DR   GeneID; 66136065; -.
DR   KEGG; mma:MM_2428; -.
DR   PATRIC; fig|192952.21.peg.2779; -.
DR   eggNOG; arCOG03402; Archaea.
DR   HOGENOM; CLU_082102_0_0_2; -.
DR   OMA; IDEGIMI; -.
DR   Proteomes; UP000000595; Chromosome.
DR   GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProt.
DR   Gene3D; 1.10.1240.10; -; 1.
DR   InterPro; IPR003759; Cbl-bd_cap.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR036724; Cobalamin-bd_sf.
DR   InterPro; IPR036594; Meth_synthase_dom.
DR   Pfam; PF02310; B12-binding; 1.
DR   Pfam; PF02607; B12-binding_2; 1.
DR   SMART; SM01018; B12-binding_2; 1.
DR   SUPFAM; SSF47644; SSF47644; 1.
DR   SUPFAM; SSF52242; SSF52242; 1.
DR   PROSITE; PS51332; B12_BINDING; 1.
DR   PROSITE; PS51337; B12_BINDING_NTER; 1.
PE   3: Inferred from homology;
KW   Cobalt; Metal-binding; Reference proteome.
FT   CHAIN           1..275
FT                   /note="Methylated-thiol--corrinoid protein MtsB"
FT                   /id="PRO_0000419109"
FT   DOMAIN          53..147
FT                   /note="B12-binding N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00667"
FT   DOMAIN          145..272
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00666"
FT   BINDING         158
FT                   /ligand="methylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:28115"
FT                   /ligand_part="Co"
FT                   /ligand_part_id="ChEBI:CHEBI:27638"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   275 AA;  29878 MW;  8999E123A2A5B1E4 CRC64;
     MIRHIDIAVQ KIFEMKEKEP AKFKKLIDEG IMIGLGVDLG DRSREEYTAG HIKEQSRPKD
     PDYAAVTEAV IEGDSEETVR LTVALLEKGK DPTDLVLNAL MPGIQTVCEL YDIGESYMPE
     ILLANEALIG GVKLCQERIG EIRYEGKVVS LVIEGDLHDI GKNIVAAILR ANGFEVVDLG
     NDITVEAAVK AVKAANADLV VGTTLMSTTK EGLKVLAEVL ESEDVPVACG GAAVDRRFVE
     TFCNSVYGKT PLDAVKIAKN ICAGKSWKEV RNDLH