RSMB_PSEAE
ID RSMB_PSEAE Reviewed; 434 AA.
AC Q9I7A9;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, 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; OrderedLocusNames=PA0017;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AE004091; AAG03407.1; -; Genomic_DNA.
DR PIR; F83643; F83643.
DR RefSeq; NP_248707.1; NC_002516.2.
DR RefSeq; WP_003114643.1; NZ_QZGE01000012.1.
DR AlphaFoldDB; Q9I7A9; -.
DR SMR; Q9I7A9; -.
DR STRING; 287.DR97_2970; -.
DR PaxDb; Q9I7A9; -.
DR PRIDE; Q9I7A9; -.
DR DNASU; 879297; -.
DR EnsemblBacteria; AAG03407; AAG03407; PA0017.
DR GeneID; 879297; -.
DR KEGG; pae:PA0017; -.
DR PATRIC; fig|208964.12.peg.16; -.
DR PseudoCAP; PA0017; -.
DR HOGENOM; CLU_005316_0_4_6; -.
DR InParanoid; Q9I7A9; -.
DR OMA; RVNRQHH; -.
DR PhylomeDB; Q9I7A9; -.
DR BioCyc; PAER208964:G1FZ6-17-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009383; F:rRNA (cytosine-C5-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central.
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..434
FT /note="Ribosomal RNA small subunit methyltransferase B"
FT /id="PRO_0000211799"
FT ACT_SITE 373
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 251..257
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 275
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 301
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 320
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 434 AA; 47154 MW; 53DC95798D57DCB0 CRC64;
MNPRLAACQA LAAVLAGRAS LSGALPPQLD KVAPRDRGLT QELAFGAARW QPRLQALAAR
LLQKPFKAAD TDIHALLLIG LYQLLYTRIP PHAAIGETVG CADKLKKGWA KGVLNAVLRR
AQREGETLLA EVDRDPSARL GHPRWLLKAL KQAWPEQLDA LCAANNAHPP MTLRVNRRHG
ERDAYLAELA EAGIKARACD YSRDGIQLAA PRDVRELPGF AEGRVSVQDE AAQLAAEQLE
SAPGQRVLDA CCAPGGKTCH LLETQPELAE VVAVDLEESR LVRVRENLQR LGLQASLVAA
DARATGEWWD GKPFQRILLD APCSATGVIR RHPDIKLARK PEDIAALAHL QGELLDALWP
TLEVGGVLLY ATCSVMPAEN SDSIAAFLAR TPGARELDLP GPWGMKQPHG RQLLPQVEGH
DGFYYAKLIK ISAR
