ID   RSMB_ERWT9              Reviewed;         429 AA.
AC   B2VK95;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase B {ECO:0000255|HAMAP-Rule:MF_01856};
DE            EC=2.1.1.176 {ECO:0000255|HAMAP-Rule:MF_01856};
DE   AltName: Full=16S rRNA m5C967 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01856};
DE   AltName: Full=rRNA (cytosine-C(5)-)-methyltransferase RsmB {ECO:0000255|HAMAP-Rule:MF_01856};
GN   Name=rsmB {ECO:0000255|HAMAP-Rule:MF_01856};
GN   Synonyms=sun {ECO:0000255|HAMAP-Rule:MF_01856};
GN   OrderedLocusNames=ETA_31300;
OS   Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS   4357 / Et1/99).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=465817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99;
RX   PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA   Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA   Geider K.;
RT   "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT   bacterium in the genus Erwinia.";
RL   Environ. Microbiol. 10:2211-2222(2008).
CC   -!- FUNCTION: Specifically methylates the cytosine at position 967 (m5C967)
CC       of 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_01856}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_01856};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01856}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000255|HAMAP-Rule:MF_01856}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU468135; CAO98176.1; -; Genomic_DNA.
DR   RefSeq; WP_012442824.1; NC_010694.1.
DR   AlphaFoldDB; B2VK95; -.
DR   SMR; B2VK95; -.
DR   STRING; 465817.ETA_31300; -.
DR   EnsemblBacteria; CAO98176; CAO98176; ETA_31300.
DR   KEGG; eta:ETA_31300; -.
DR   eggNOG; COG0144; Bacteria.
DR   eggNOG; COG0781; Bacteria.
DR   HOGENOM; CLU_005316_0_4_6; -.
DR   OMA; RVNRQHH; -.
DR   OrthoDB; 1064993at2; -.
DR   Proteomes; UP000001726; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016434; F:rRNA (cytosine) methyltransferase activity; IEA:UniProtKB-UniRule.
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   HAMAP; MF_01856; 16SrRNA_methyltr_B; 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; IPR023541; rRNA_ssu_MeTfrase_B_ent.
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; RNA-binding;
KW   rRNA processing; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..429
FT                   /note="Ribosomal RNA small subunit methyltransferase B"
FT                   /id="PRO_0000366150"
FT   ACT_SITE        375
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01856"
FT   BINDING         254..260
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01856"
FT   BINDING         277
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01856"
FT   BINDING         303
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01856"
FT   BINDING         322
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01856"
SQ   SEQUENCE   429 AA;  47864 MW;  3DD9BB9DC7F0D5A9 CRC64;
     MKKMTNLRCI AAQTIEKVVE QGQSLSNVLP AAQKSVGDKD AALLQELCYG VLRTLPQLEW
     VIGRLMSRPM TGKQRAVHFL IMVGLYQLMF TRIPAHAALA ETVEGAVALK RPQLKGLING
     VLRQFQRQQD ELMQQMNDGD QQYLHPKWLL ERLKRAWPAQ WKQIVDANNQ RPPMWLRVNR
     QHHSRDAWLT LLEESGKQAF AHPQHGDALR LESPCAVGQL PGFDQGWITV QDVSAQGCVA
     LLAPRDGEQI LDLCAAPGGK TTHILEAAPQ AKVMAVDVDA QRLARVSENL QRLTMQAEVK
     QGDGRTPAAW CGDTQFDRIL LDAPCSATGV IRRHPDIKWL RRDRDIAELA ALQQQILDAV
     WPHLKPGGTL LYATCSVLPE ENHVQIGQFL QRHADATLIE TGDLTQPGIQ VFPQADGGDG
     FYYAKLVKQ