ID   MTSB_METBA              Reviewed;         275 AA.
AC   Q48925;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Methylated-thiol--corrinoid protein MtsB;
DE   AltName: Full=Methylthiol:coenzyme M methyltransferase 30 kDa subunit;
GN   Name=mtsB;
OS   Methanosarcina barkeri.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=2208;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474;
RX   PubMed=8932317; DOI=10.1128/jb.178.22.6599-6607.1996;
RA   Paul L., Krzycki J.A.;
RT   "Sequence and transcript analysis of a novel Methanosarcina barkeri
RT   methyltransferase II homolog and its associated corrinoid protein
RT   homologous to methionine synthase.";
RL   J. Bacteriol. 178:6599-6607(1996).
RN   [2]
RP   FUNCTION.
RC   STRAIN=ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474;
RX   PubMed=11073950; DOI=10.1074/jbc.m007514200;
RA   Tallant T.C., Paul L., Krzycki J.A.;
RT   "The MtsA subunit of the methylthiol:coenzyme M methyltransferase of
RT   Methanosarcina barkeri catalyses both half-reactions of corrinoid-dependent
RT   dimethylsulfide: coenzyme M methyl transfer.";
RL   J. Biol. Chem. 276:4485-4493(2001).
CC   -!- FUNCTION: Harbors a corrinoid prosthetic group and acts as a methyl
CC       group carrier in methanogenesis from methylated-thiols.
CC       {ECO:0000269|PubMed:11073950}.
CC   -!- SIMILARITY: Belongs to the methylamine corrinoid protein family.
CC       {ECO:0000305}.
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DR   EMBL; U36337; AAC46231.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q48925; -.
DR   SMR; Q48925; -.
DR   BioCyc; MetaCyc:MON-12242; -.
DR   GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044683; F:methylthiol:coenzyme M methyltransferase activity; IDA:MENGO.
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.
FT   CHAIN           1..275
FT                   /note="Methylated-thiol--corrinoid protein MtsB"
FT                   /id="PRO_0000419108"
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;  29612 MW;  C5F0694549ECABB2 CRC64;
     MIRHIDLAVQ NILEMKEKEP AKFKRLIDEG IMIGLGVDLE DGNKEVTTVD QIKNQNRPKD
     PEYASVAEAV IEGNNAETVK LISALLEKGK DPTDLVLNAL MPGIQTVCEL YDIGESYVPE
     ILLANEALMK GVELCQKKKG EVPSQGKVVS LVIVGDLHDI GKNIVAAILR ANGFEVIDLG
     RDVTVEAAVE AVKSTKANLV TGTTLMSTTK GGLKALANAL EPEGVPLACG GAAVDRRFVD
     TFGNSVYGRT PLDAVKIAKE ICEGKSWEEA RNELY