ID   Y4108_BACHK             Reviewed;         212 AA.
AC   Q6HDF0;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Uncharacterized methyltransferase BT9727_4108 {ECO:0000255|HAMAP-Rule:MF_02100};
DE            EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_02100};
GN   OrderedLocusNames=BT9727_4108;
OS   Bacillus thuringiensis subsp. konkukian (strain 97-27).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=281309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=97-27;
RX   PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA   Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA   Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA   Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA   Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA   Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
CC   -!- FUNCTION: Could be a S-adenosyl-L-methionine-dependent
CC       methyltransferase. {ECO:0000255|HAMAP-Rule:MF_02100}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. YrrT family.
CC       {ECO:0000255|HAMAP-Rule:MF_02100}.
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DR   EMBL; AE017355; AAT63667.1; -; Genomic_DNA.
DR   RefSeq; WP_000536327.1; NC_005957.1.
DR   RefSeq; YP_038426.1; NC_005957.1.
DR   PDB; 3HNR; X-ray; 2.80 A; A=1-212.
DR   PDBsum; 3HNR; -.
DR   AlphaFoldDB; Q6HDF0; -.
DR   SMR; Q6HDF0; -.
DR   EnsemblBacteria; AAT63667; AAT63667; BT9727_4108.
DR   KEGG; btk:BT9727_4108; -.
DR   PATRIC; fig|281309.8.peg.4385; -.
DR   HOGENOM; CLU_111961_0_0_9; -.
DR   OMA; FEDWAAT; -.
DR   EvolutionaryTrace; Q6HDF0; -.
DR   Proteomes; UP000001301; Chromosome.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_02100; Methyltr_YrrT; 1.
DR   InterPro; IPR013216; Methyltransf_11.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR023553; Uncharacterised_MeTfrase_YrrT.
DR   Pfam; PF08241; Methyltransf_11; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..212
FT                   /note="Uncharacterized methyltransferase BT9727_4108"
FT                   /id="PRO_0000373850"
FT   BINDING         53
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02100"
FT   BINDING         74
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02100"
FT   BINDING         97
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02100"
FT   TURN            26..33
FT                   /evidence="ECO:0007829|PDB:3HNR"
FT   HELIX           34..43
FT                   /evidence="ECO:0007829|PDB:3HNR"
FT   STRAND          47..52
FT                   /evidence="ECO:0007829|PDB:3HNR"
FT   HELIX           58..65
FT                   /evidence="ECO:0007829|PDB:3HNR"
FT   STRAND          69..73
FT                   /evidence="ECO:0007829|PDB:3HNR"
FT   HELIX           77..86
FT                   /evidence="ECO:0007829|PDB:3HNR"
FT   STRAND          93..95
FT                   /evidence="ECO:0007829|PDB:3HNR"
FT   STRAND          98..100
FT                   /evidence="ECO:0007829|PDB:3HNR"
FT   STRAND          108..114
FT                   /evidence="ECO:0007829|PDB:3HNR"
FT   HELIX           116..118
FT                   /evidence="ECO:0007829|PDB:3HNR"
FT   HELIX           121..134
FT                   /evidence="ECO:0007829|PDB:3HNR"
FT   STRAND          140..146
FT                   /evidence="ECO:0007829|PDB:3HNR"
FT   STRAND          148..150
FT                   /evidence="ECO:0007829|PDB:3HNR"
FT   HELIX           151..163
FT                   /evidence="ECO:0007829|PDB:3HNR"
FT   HELIX           167..175
FT                   /evidence="ECO:0007829|PDB:3HNR"
FT   HELIX           181..190
FT                   /evidence="ECO:0007829|PDB:3HNR"
FT   STRAND          193..199
FT                   /evidence="ECO:0007829|PDB:3HNR"
FT   STRAND          201..211
FT                   /evidence="ECO:0007829|PDB:3HNR"
SQ   SEQUENCE   212 AA;  24264 MW;  D71ABBD0AF5F94DC CRC64;
     MGTEFNGLFD EWAHTYDSFV QGEDIQYKEV FAHYEDILED VVNKSFGNVL EFGVGTGNLT
     NKLLLAGRTV YGIEPSREMR MIAKEKLPKE FSITEGDFLS FEVPTSIDTI VSTYAFHHLT
     DDEKNVAIAK YSQLLNKGGK IVFADTIFAD QDAYDKTVEA AKQRGFHQLA NDLQTEYYTR
     IPVMQTIFEN NGFHVTFTRL NHFVWVMEAT KQ