RSMI_ECOLI
ID RSMI_ECOLI Reviewed; 286 AA.
AC P67087; P45528; Q2M964;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase I;
DE EC=2.1.1.198;
DE AltName: Full=16S rRNA 2'-O-ribose C1402 methyltransferase;
DE AltName: Full=rRNA (cytidine-2'-O-)-methyltransferase RsmI;
GN Name=rsmI; Synonyms=yraL; OrderedLocusNames=b3146, JW3115;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=K12;
RX PubMed=19965768; DOI=10.1093/nar/gkp1073;
RA Kimura S., Suzuki T.;
RT "Fine-tuning of the ribosomal decoding center by conserved methyl-
RT modifications in the Escherichia coli 16S rRNA.";
RL Nucleic Acids Res. 38:1341-1352(2010).
CC -!- FUNCTION: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402
CC (C1402) in 16S rRNA. In vitro, active on the assembled 30S subunit, but
CC not naked 16S rRNA or 70S ribosomes. {ECO:0000269|PubMed:19965768}.
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:0000269|PubMed:19965768};
CC -!- INTERACTION:
CC P67087; P06959: aceF; NbExp=2; IntAct=EBI-561394, EBI-542707;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmI family.
CC {ECO:0000305}.
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DR EMBL; U18997; AAA57949.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76180.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77192.1; -; Genomic_DNA.
DR PIR; F65104; F65104.
DR RefSeq; NP_417615.1; NC_000913.3.
DR RefSeq; WP_000809262.1; NZ_STEB01000012.1.
DR PDB; 5HW4; X-ray; 2.21 A; A/B/C=12-258.
DR PDBsum; 5HW4; -.
DR AlphaFoldDB; P67087; -.
DR SMR; P67087; -.
DR BioGRID; 4261593; 91.
DR DIP; DIP-12896N; -.
DR IntAct; P67087; 3.
DR STRING; 511145.b3146; -.
DR jPOST; P67087; -.
DR PaxDb; P67087; -.
DR PRIDE; P67087; -.
DR EnsemblBacteria; AAC76180; AAC76180; b3146.
DR EnsemblBacteria; BAE77192; BAE77192; BAE77192.
DR GeneID; 58462813; -.
DR GeneID; 947664; -.
DR KEGG; ecj:JW3115; -.
DR KEGG; eco:b3146; -.
DR PATRIC; fig|1411691.4.peg.3584; -.
DR EchoBASE; EB2630; -.
DR eggNOG; COG0313; Bacteria.
DR HOGENOM; CLU_044779_4_0_6; -.
DR InParanoid; P67087; -.
DR OMA; RTMVFFE; -.
DR PhylomeDB; P67087; -.
DR BioCyc; EcoCyc:G7641-MON; -.
DR BioCyc; MetaCyc:G7641-MON; -.
DR BRENDA; 2.1.1.198; 2026.
DR PRO; PR:P67087; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070677; F:rRNA (cytosine-2'-O-)-methyltransferase activity; IDA:EcoCyc.
DR GO; GO:0000453; P:enzyme-directed rRNA 2'-O-methylation; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..286
FT /note="Ribosomal RNA small subunit methyltransferase I"
FT /id="PRO_0000211938"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:5HW4"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:5HW4"
FT HELIX 29..37
FT /evidence="ECO:0007829|PDB:5HW4"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:5HW4"
FT HELIX 46..55
FT /evidence="ECO:0007829|PDB:5HW4"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:5HW4"
FT HELIX 71..82
FT /evidence="ECO:0007829|PDB:5HW4"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:5HW4"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:5HW4"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:5HW4"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:5HW4"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:5HW4"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:5HW4"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:5HW4"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:5HW4"
FT HELIX 149..158
FT /evidence="ECO:0007829|PDB:5HW4"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:5HW4"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:5HW4"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:5HW4"
FT HELIX 175..186
FT /evidence="ECO:0007829|PDB:5HW4"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:5HW4"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:5HW4"
FT HELIX 210..219
FT /evidence="ECO:0007829|PDB:5HW4"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:5HW4"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:5HW4"
SQ SEQUENCE 286 AA; 31348 MW; 886EA492858FB95C CRC64;
MKQHQSADNS QGQLYIVPTP IGNLADITQR ALEVLQAVDL IAAEDTRHTG LLLQHFGINA
RLFALHDHNE QQKAETLLAK LQEGQNIALV SDAGTPLIND PGYHLVRTCR EAGIRVVPLP
GPCAAITALS AAGLPSDRFC YEGFLPAKSK GRRDALKAIE AEPRTLIFYE STHRLLDSLE
DIVAVLGESR YVVLARELTK TWETIHGAPV GELLAWVKED ENRRKGEMVL IVEGHKAQEE
DLPADALRTL ALLQAELPLK KAAALAAEIH GVKKNALYKY ALEQQG
