RSMB_THET8
ID RSMB_THET8 Reviewed; 398 AA.
AC Q5SK01;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase B {ECO:0000250|UniProtKB:P36929};
DE EC=2.1.1.176 {ECO:0000269|PubMed:20558545};
DE AltName: Full=16S rRNA m5C967 methyltransferase {ECO:0000250|UniProtKB:P36929};
DE AltName: Full=rRNA (cytosine-C(5)-)-methyltransferase RsmB {ECO:0000250|UniProtKB:P36929};
GN Name=rsmB {ECO:0000303|PubMed:20558545};
GN OrderedLocusNames=TTHA0851 {ECO:0000312|EMBL:BAD70674.1};
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=20558545; DOI=10.1261/rna.2088310;
RA Demirci H., Larsen L.H., Hansen T., Rasmussen A., Cadambi A., Gregory S.T.,
RA Kirpekar F., Jogl G.;
RT "Multi-site-specific 16S rRNA methyltransferase RsmF from Thermus
RT thermophilus.";
RL RNA 16:1584-1596(2010).
CC -!- FUNCTION: Specifically methylates the cytosine at position 967 (m5C967)
CC of 16S rRNA. {ECO:0000269|PubMed:20558545}.
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:0000269|PubMed:20558545};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P36929}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000255|PROSITE-ProRule:PRU01023}.
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; AP008226; BAD70674.1; -; Genomic_DNA.
DR RefSeq; WP_011228244.1; NC_006461.1.
DR RefSeq; YP_144117.1; NC_006461.1.
DR AlphaFoldDB; Q5SK01; -.
DR SMR; Q5SK01; -.
DR STRING; 300852.55772233; -.
DR EnsemblBacteria; BAD70674; BAD70674; BAD70674.
DR GeneID; 3170008; -.
DR KEGG; ttj:TTHA0851; -.
DR PATRIC; fig|300852.9.peg.845; -.
DR eggNOG; COG0144; Bacteria.
DR HOGENOM; CLU_005316_0_4_0; -.
DR OMA; RVNRQHH; -.
DR PhylomeDB; Q5SK01; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 1.10.940.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR InterPro; IPR035926; NusB-like_sf.
DR InterPro; IPR006027; NusB_RsmB_TIM44.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22807; PTHR22807; 2.
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 PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Reference proteome; RNA-binding;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..398
FT /note="Ribosomal RNA small subunit methyltransferase B"
FT /id="PRO_0000431480"
FT ACT_SITE 336
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 221..227
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P36929"
FT BINDING 242
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P36929"
FT BINDING 268
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P36929"
FT BINDING 283
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P36929"
SQ SEQUENCE 398 AA; 44312 MW; 60BD5FB94549F335 CRC64;
MRAGTPRALA VAVLLEVDRG GRAQLLLDRA LRRSPWPERD RAYATFLVYG ALRRLRLLDH
LLAPLLPRPE GLPPEVRWIL RLGALEWLEG KPDHARVSPW VEEAKRRYPG LAGLVNAVLR
RLAPREAPEC VRLSLPDWLC EAWRGFFGDV AFAEGFNEPA PLFVTAYREV DLRPGPVPGS
YLWEGPKTDF SALGLQPQNP ASLFAAKLLE ARPGERVLDL CGGAGLKAFY LAAQGAEVVS
YDLNRRRQEA GARTARRLGL WVHYRTQDLT RPVPERAKKV LLDAPCTGTG TFRAHPELRY
RLSPEDPARM AALQLQLLET AAQATEEGGV LVYSVCTLTE EEGEGVVRAF LARHPEFRPE
PVQPPFPVLA RGLGVYVDPR GGLDGFYYAK LRRVNSQA
