RSMI_STRPQ
ID RSMI_STRPQ Reviewed; 287 AA.
AC P0DF47; Q79WD8; Q8K8H1;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase I {ECO:0000255|HAMAP-Rule:MF_01877};
DE EC=2.1.1.198 {ECO:0000255|HAMAP-Rule:MF_01877};
DE AltName: Full=16S rRNA 2'-O-ribose C1402 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01877};
DE AltName: Full=rRNA (cytidine-2'-O-)-methyltransferase RsmI {ECO:0000255|HAMAP-Rule:MF_01877};
GN Name=rsmI {ECO:0000255|HAMAP-Rule:MF_01877}; OrderedLocusNames=SPs1565;
OS Streptococcus pyogenes serotype M3 (strain SSI-1).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=193567;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSI-1;
RX PubMed=12799345; DOI=10.1101/gr.1096703;
RA Nakagawa I., Kurokawa K., Yamashita A., Nakata M., Tomiyasu Y.,
RA Okahashi N., Kawabata S., Yamazaki K., Shiba T., Yasunaga T., Hayashi H.,
RA Hattori M., Hamada S.;
RT "Genome sequence of an M3 strain of Streptococcus pyogenes reveals a large-
RT scale genomic rearrangement in invasive strains and new insights into phage
RT evolution.";
RL Genome Res. 13:1042-1055(2003).
CC -!- FUNCTION: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402
CC (C1402) in 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_01877}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-
CC methylcytidine(1402) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42924, Rhea:RHEA-COMP:10285, Rhea:RHEA-COMP:10286,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; EC=2.1.1.198;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01877};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01877}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmI family.
CC {ECO:0000255|HAMAP-Rule:MF_01877}.
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DR EMBL; BA000034; BAC64660.1; -; Genomic_DNA.
DR RefSeq; WP_011054222.1; NC_004606.1.
DR AlphaFoldDB; P0DF47; -.
DR SMR; P0DF47; -.
DR KEGG; sps:SPs1565; -.
DR HOGENOM; CLU_044779_1_0_9; -.
DR OMA; RTMVFFE; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070677; F:rRNA (cytosine-2'-O-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000453; P:enzyme-directed rRNA 2'-O-methylation; IEA:UniProtKB-UniRule.
DR CDD; cd11648; RsmI; 1.
DR Gene3D; 3.30.950.10; -; 1.
DR Gene3D; 3.40.1010.10; -; 1.
DR HAMAP; MF_01877; 16SrRNA_methyltr_I; 1.
DR InterPro; IPR000878; 4pyrrol_Mease.
DR InterPro; IPR035996; 4pyrrol_Methylase_sf.
DR InterPro; IPR014777; 4pyrrole_Mease_sub1.
DR InterPro; IPR014776; 4pyrrole_Mease_sub2.
DR InterPro; IPR008189; rRNA_ssu_MeTfrase_I.
DR InterPro; IPR018063; SAM_MeTrfase_RsmI_CS.
DR PANTHER; PTHR46111; PTHR46111; 1.
DR Pfam; PF00590; TP_methylase; 1.
DR PIRSF; PIRSF005917; MTase_YraL; 1.
DR SUPFAM; SSF53790; SSF53790; 1.
DR TIGRFAMs; TIGR00096; TIGR00096; 1.
DR PROSITE; PS01296; RSMI; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; rRNA processing; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..287
FT /note="Ribosomal RNA small subunit methyltransferase I"
FT /id="PRO_0000411563"
SQ SEQUENCE 287 AA; 31866 MW; 66A6F0E9FE114140 CRC64;
MQVQKSFKDK KTSGTLYLVP TPIGNLQDMT FRAVATLKEV DFICAEDTRN TGLLLKHFDI
ATKQISFHEH NAYEKIPDLI DLLISGRSLA QVSDAGMPSI SDPGHDLVKA AIDSDITVVA
LPGASAGITA LIASGLAPQP HVFYGFLPRK AGQQKAFFED KHHYPETQMF YESPYRIKDT
LTNMLACYGD RQVVLVRELT KLFEEYQRGS ISEILSYLEE TSLKGECLLI VAGAQVDSEV
ELTADVDLVS LVQKEIQAGA KPNQAIKTIA KAYQVNRQEL YQQFHDL
