ID   RSMB_VIBVY              Reviewed;         426 AA.
AC   Q7MGK4;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase B;
DE            EC=2.1.1.176;
DE   AltName: Full=16S rRNA m5C967 methyltransferase;
DE   AltName: Full=rRNA (cytosine-C(5)-)-methyltransferase RsmB;
GN   Name=rsmB; Synonyms=rrmB; OrderedLocusNames=VV3227;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
CC   -!- FUNCTION: Specifically methylates the cytosine at position 967 (m5C967)
CC       of 16S rRNA. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cytidine(967) in 16S rRNA + S-adenosyl-L-methionine = 5-
CC         methylcytidine(967) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42748, Rhea:RHEA-COMP:10219, Rhea:RHEA-COMP:10220,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; EC=2.1.1.176;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000255|PROSITE-ProRule:PRU01023}.
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DR   EMBL; BA000037; BAC95991.1; -; Genomic_DNA.
DR   RefSeq; WP_011151424.1; NC_005139.1.
DR   AlphaFoldDB; Q7MGK4; -.
DR   SMR; Q7MGK4; -.
DR   STRING; 672.VV93_v1c29490; -.
DR   PRIDE; Q7MGK4; -.
DR   EnsemblBacteria; BAC95991; BAC95991; BAC95991.
DR   KEGG; vvy:VV3227; -.
DR   PATRIC; fig|196600.6.peg.3193; -.
DR   eggNOG; COG0144; Bacteria.
DR   eggNOG; COG0781; Bacteria.
DR   HOGENOM; CLU_005316_0_4_6; -.
DR   OMA; RVNRQHH; -.
DR   OrthoDB; 1064993at2; -.
DR   Proteomes; UP000002675; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008649; F:rRNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.940.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR   InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR   InterPro; IPR035926; NusB-like_sf.
DR   InterPro; IPR006027; NusB_RsmB_TIM44.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR004573; rRNA_ssu_MeTfrase_B.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22807; PTHR22807; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   Pfam; PF01029; NusB; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF48013; SSF48013; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00563; rsmB; 1.
DR   PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Reference proteome; Ribosome biogenesis;
KW   RNA-binding; rRNA processing; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..426
FT                   /note="Ribosomal RNA small subunit methyltransferase B"
FT                   /id="PRO_0000211809"
FT   ACT_SITE        372
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT   BINDING         251..257
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT   BINDING         274
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT   BINDING         300
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT   BINDING         319
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   426 AA;  47688 MW;  D5320602762A1DFC CRC64;
     MNVRAAAANV LYQVVDRGNS LSTALPEAQQ SIRPRDHALL QEICYGALRY LPRLESIAGK
     LMDKPLKGKQ RVFHHLILVG LYQLGHMRIP AHAAVGETVE GAQALKGPRL RGLINAVLRN
     YQREQQALDE FSVSHNAGKY VHPSWLLKIL QDAYPEQWQT IVEANNNKAP MWLRVNHAHH
     DRDEYLQLLK NANIDSTLHS EAMDAIKLAA PCDVHSLPGF EQGWVSVQDA AAQLSFNYLQ
     PKDGELILDC CAAPGGKTAH ILERVSAREV VALDCDEQRL KRVTENLKRL NLQAKVICGD
     ARNPEQWWQG EQFDRILLDA PCSATGVIRR HPDIKWLRRA EDITALAQLQ SEIFDAMWAQ
     LKPGGTLVYA TCSITPMENV EQVKAFLART PAAQLVGSER ENPGRQILPG EEDMDGFYYA
     VLVKQA