ID   RSMB_HAEDU              Reviewed;         435 AA.
AC   Q7VKC4;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=HD_1992;
OS   Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=233412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RA   Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA   Nguyen D., Wang J., Forst C., Hood L.;
RT   "The complete genome sequence of Haemophilus ducreyi.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
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; AE017143; AAP96708.1; -; Genomic_DNA.
DR   RefSeq; WP_010945729.1; NC_002940.2.
DR   AlphaFoldDB; Q7VKC4; -.
DR   SMR; Q7VKC4; -.
DR   STRING; 233412.HD_1992; -.
DR   EnsemblBacteria; AAP96708; AAP96708; HD_1992.
DR   KEGG; hdu:HD_1992; -.
DR   eggNOG; COG0144; Bacteria.
DR   HOGENOM; CLU_005316_0_4_6; -.
DR   OMA; RVNRQHH; -.
DR   Proteomes; UP000001022; 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..435
FT                   /note="Ribosomal RNA small subunit methyltransferase B"
FT                   /id="PRO_0000211796"
FT   ACT_SITE        377
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT   BINDING         255..261
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT   BINDING         278
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT   BINDING         304
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT   BINDING         324
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   435 AA;  48720 MW;  795C28EF74A9E457 CRC64;
     MKHKKTSSRA IAAQIMLQVL DHGKSLSTLI PAAQQQLDAK DIPLVQEITF GICRVLPRLE
     AIIQQLVTKP LKGKSRLVHC LLLVGLYQLL YMRIPVHAAV DEVVNATKLV KLDSFRALTN
     GVLRRFLREQ QTILAKVDKH WQTLHPEWLV NMLKQVYPNW REIMDANNQR PPMWIRVNTQ
     HCTPQDYSAL LGDLAVKTTN SSACLPSSAI QLVNPLSVDK LPYFSRGWAT VQDCHAQWSA
     TLLAAKNGEM ILDACAAPGG KTTHILEQAP QAKVIALDIE ESRLVRVREN LARLGLTADV
     RCGDATTPTK WLADDVMFDR ILLDAPCSAT GVIRRHPDIK WLRQAGDISE LVELQAKILS
     ALWHRLKPNG TLVYATCSIL PAENSEQIIQ FITANPDAEL IEMDFNGEKA IMKQFLPQQN
     GGDGFFYAKL RKLDK