ID   Y4369_BACCR             Reviewed;         212 AA.
AC   Q818A1;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Uncharacterized methyltransferase BC_4369 {ECO:0000255|HAMAP-Rule:MF_02100};
DE            EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_02100};
GN   OrderedLocusNames=BC_4369;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAP11282.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AE016877; AAP11282.1; ALT_FRAME; Genomic_DNA.
DR   RefSeq; NP_834081.1; NC_004722.1.
DR   RefSeq; WP_000536320.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q818A1; -.
DR   SMR; Q818A1; -.
DR   STRING; 226900.BC_4369; -.
DR   EnsemblBacteria; AAP11282; AAP11282; BC_4369.
DR   KEGG; bce:BC4369; -.
DR   PATRIC; fig|226900.8.peg.4519; -.
DR   HOGENOM; CLU_111961_0_0_9; -.
DR   OMA; FEDWAAT; -.
DR   Proteomes; UP000001417; Chromosome.
DR   GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
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   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..212
FT                   /note="Uncharacterized methyltransferase BC_4369"
FT                   /id="PRO_0000373843"
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"
SQ   SEQUENCE   212 AA;  24308 MW;  9FA6D176E2E0A835 CRC64;
     MGTEFNGLFD EWAHTYDSFV QGEDIQYKEV FAHYEDILED VVNKSFGNVL EFGVGTGNLT
     NKLLLAGRTV YGIEPSREMR MIAKEKLPKE FSITEGDFLS FEVPNSIDTI VSTYAFHHLT
     DDEKNVAIAK YSQLLNKGGK IVFADTIFAD QDAYDKTVET AKERGFHQLA NDLQTEYYTR
     IPVMQTIFEN NGFHVTFTRL NHFVWVMEAT KQ