RSMB_SALPC
ID RSMB_SALPC Reviewed; 429 AA.
AC C0PZV1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
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}; OrderedLocusNames=SPC_3477;
OS Salmonella paratyphi C (strain RKS4594).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=476213;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RKS4594;
RX PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT and pathogenic convergence with Salmonella typhi.";
RL PLoS ONE 4:E4510-E4510(2009).
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}.
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DR EMBL; CP000857; ACN47561.1; -; Genomic_DNA.
DR RefSeq; WP_000744608.1; NC_012125.1.
DR AlphaFoldDB; C0PZV1; -.
DR SMR; C0PZV1; -.
DR EnsemblBacteria; ACN47561; ACN47561; SPC_3477.
DR KEGG; sei:SPC_3477; -.
DR HOGENOM; CLU_005316_0_4_6; -.
DR OMA; RVNRQHH; -.
DR Proteomes; UP000001599; 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; RNA-binding; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..429
FT /note="Ribosomal RNA small subunit methyltransferase B"
FT /id="PRO_1000188697"
FT REGION 397..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 48100 MW; 7659006A4A90E8F7 CRC64;
MKKQNNLRSL AAQAVEQVVE QGQSLSNVLP PLQQKVADKD KALLQELCFG VLRTLSQLEW
LINKLMSRPM TGKQRTVHYL IMVGFYQLLY TRVPPHAALA ETVEGAVSIK RPQLKGLING
VLRQFQRQQE TLLNEFATSD ARFLHPGWLV KRLQNAYPTQ WQRIIDANNQ RPPMWLRVNR
THHTRDGWLG LLEDAGMKGY PHPDYPDAVR LETPAPVHAL PGFAEGWVTV QDASAQGCAV
FLAPQNGEHI LDLCAAPGGK TTHILEVAPE ADVLAVDIDE QRLSRVYDNL KRLGMKATVK
QGDGRYPAQW CGEQQFDRIL LDAPCSATGV IRRHPDIKWL RRDRDIAELA QLQAEILDAV
WPRLKPGGTL VYATCSVLPE ENRDQIKTFL QRTPDAALSE TGTPDQPGQQ NLPGGEEGDG
FFYAKLIKK