ID   RSMB_PASMU              Reviewed;         446 AA.
AC   Q9CKP7;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 121.
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, sun; OrderedLocusNames=PM1561;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK03645.1; -; Genomic_DNA.
DR   RefSeq; WP_010907231.1; NC_002663.1.
DR   AlphaFoldDB; Q9CKP7; -.
DR   SMR; Q9CKP7; -.
DR   STRING; 747.DR93_409; -.
DR   EnsemblBacteria; AAK03645; AAK03645; PM1561.
DR   KEGG; pmu:PM1561; -.
DR   PATRIC; fig|272843.6.peg.1578; -.
DR   HOGENOM; CLU_005316_0_4_6; -.
DR   OMA; RVNRQHH; -.
DR   Proteomes; UP000000809; Chromosome.
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..446
FT                   /note="Ribosomal RNA small subunit methyltransferase B"
FT                   /id="PRO_0000211797"
FT   ACT_SITE        387
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT   BINDING         261..267
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT   BINDING         284
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT   BINDING         310
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT   BINDING         334
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   446 AA;  49885 MW;  424C18ADA6011B44 CRC64;
     MQKFVKNVKK QTVLLSTRAI AAQIILQVLD QGKSLSTLIP DTQHQVKTQD LPLLQEICFG
     VCRVLPRLEL IIKQLVDKPL KGKTRIVHCL LLVGLYQLLY TRIPAHAAVD EVVNATTALK
     AEHFRGLVNG VLRRFLREQE TLLVKVDKHW HTLHPDWLVN RLKEAYPNWR EIVEANNHKP
     PMWLRVNQQK NSTETYRTLL AEQGIEAEKA DNPCALRLLQ PVAVSQLPAF HEGAVSVQDV
     NAQWSALLLA PENGELILDA CAAPGGKTTH ILEQAPQAHV VALDVEATRL KRVHENLARM
     QQQATVICGD ATQPAQWLKQ LSESAVQFDR ILLDAPCSAT GVIRRHPDIK WLRQASDISA
     LVALQKQILQ ALWTVLKPNG ILLYATCSVL PEENALQIEQ FLTNNVDAKL EPLPFTAVEG
     SVGYQFLPTE NGGDGFYYAK LRKVVS