RSME_ECOLI
ID RSME_ECOLI Reviewed; 243 AA.
AC P0AGL7; P37912; P76647; Q2M9P7;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase E;
DE EC=2.1.1.193;
DE AltName: Full=16S rRNA m3U1498 methyltransferase;
GN Name=rsmE; Synonyms=yggJ; OrderedLocusNames=b2946, JW2913;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-128.
RC STRAIN=K12;
RX PubMed=8113204; DOI=10.1128/jb.176.5.1550-1551.1994;
RA Jekel M., Wackernagel W.;
RT "Location of the endA gene coding for endonuclease I on the physical map of
RT the Escherichia coli K-12 chromosome.";
RL J. Bacteriol. 176:1550-1551(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 127-243.
RC STRAIN=B;
RX PubMed=6393055; DOI=10.1093/nar/12.24.9299;
RA Gushima H., Yasuda S., Soeda E., Yokota M., Kondo M., Kimura A.;
RT "Complete nucleotide sequence of the E. coli glutathione synthetase gsh-
RT II.";
RL Nucleic Acids Res. 12:9299-9307(1984).
RN [5]
RP IDENTIFICATION.
RA Rudd K.E., Baum B.;
RL Unpublished observations (AUG-1994).
RN [6]
RP FUNCTION AS METHYLTRANSFERASE, AND CATALYTIC ACTIVITY.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16431987; DOI=10.1261/rna.2283106;
RA Basturea G.N., Rudd K.E., Deutscher M.P.;
RT "Identification and characterization of RsmE, the founding member of a new
RT RNA base methyltransferase family.";
RL RNA 12:426-434(2006).
RN [7]
RP FUNCTION, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17872509; DOI=10.1261/rna.700507;
RA Basturea G.N., Deutscher M.P.;
RT "Substrate specificity and properties of the Escherichia coli 16S rRNA
RT methyltransferase, RsmE.";
RL RNA 13:1969-1976(2007).
CC -!- FUNCTION: Specifically methylates the N3 position of the uracil ring of
CC uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S
CC ribosomal subunit. {ECO:0000269|PubMed:16431987,
CC ECO:0000269|PubMed:17872509}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) +
CC N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42920, Rhea:RHEA-COMP:10283, Rhea:RHEA-COMP:10284,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74502; EC=2.1.1.193;
CC Evidence={ECO:0000269|PubMed:16431987};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.0 uM for 16S rRNA within 30S ribosomal subunits
CC {ECO:0000269|PubMed:17872509};
CC KM=26.7 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:17872509};
CC pH dependence:
CC Optimum pH is 7-9. {ECO:0000269|PubMed:17872509};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17872509}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RNA methyltransferase RsmE family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA69113.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U28377; AAA69113.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75983.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77009.1; -; Genomic_DNA.
DR EMBL; X65169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X01666; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_417421.4; NC_000913.3.
DR RefSeq; WP_001222509.1; NZ_SSUR01000013.1.
DR PDB; 4E8B; X-ray; 2.25 A; A=1-243.
DR PDBsum; 4E8B; -.
DR AlphaFoldDB; P0AGL7; -.
DR SMR; P0AGL7; -.
DR BioGRID; 4259407; 22.
DR IntAct; P0AGL7; 5.
DR STRING; 511145.b2946; -.
DR jPOST; P0AGL7; -.
DR PaxDb; P0AGL7; -.
DR PRIDE; P0AGL7; -.
DR EnsemblBacteria; AAC75983; AAC75983; b2946.
DR EnsemblBacteria; BAE77009; BAE77009; BAE77009.
DR GeneID; 60901714; -.
DR GeneID; 945816; -.
DR KEGG; ecj:JW2913; -.
DR KEGG; eco:b2946; -.
DR PATRIC; fig|1411691.4.peg.3787; -.
DR EchoBASE; EB2269; -.
DR eggNOG; COG1385; Bacteria.
DR HOGENOM; CLU_067442_5_1_6; -.
DR InParanoid; P0AGL7; -.
DR OMA; TQWKGER; -.
DR PhylomeDB; P0AGL7; -.
DR BioCyc; EcoCyc:EG12366-MON; -.
DR BioCyc; MetaCyc:EG12366-MON; -.
DR BRENDA; 2.1.1.193; 2026.
DR PRO; PR:P0AGL7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070042; F:rRNA (uridine-N3-)-methyltransferase activity; IDA:EcoCyc.
DR GO; GO:0070475; P:rRNA base methylation; IMP:EcoCyc.
DR Gene3D; 3.40.1280.10; -; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR006700; rRNA_ssu_MeTrfase-E.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR PANTHER; PTHR30027; PTHR30027; 1.
DR Pfam; PF04452; Methyltrans_RNA; 1.
DR PIRSF; PIRSF015601; MTase_slr0722; 1.
DR SUPFAM; SSF75217; SSF75217; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00046; TIGR00046; 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..243
FT /note="Ribosomal RNA small subunit methyltransferase E"
FT /id="PRO_0000176199"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:4E8B"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:4E8B"
FT HELIX 22..29
FT /evidence="ECO:0007829|PDB:4E8B"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:4E8B"
FT STRAND 45..57
FT /evidence="ECO:0007829|PDB:4E8B"
FT STRAND 62..71
FT /evidence="ECO:0007829|PDB:4E8B"
FT STRAND 77..85
FT /evidence="ECO:0007829|PDB:4E8B"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:4E8B"
FT HELIX 91..101
FT /evidence="ECO:0007829|PDB:4E8B"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:4E8B"
FT HELIX 121..142
FT /evidence="ECO:0007829|PDB:4E8B"
FT HELIX 156..161
FT /evidence="ECO:0007829|PDB:4E8B"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:4E8B"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:4E8B"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:4E8B"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:4E8B"
FT HELIX 201..209
FT /evidence="ECO:0007829|PDB:4E8B"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:4E8B"
FT HELIX 224..238
FT /evidence="ECO:0007829|PDB:4E8B"
SQ SEQUENCE 243 AA; 26978 MW; 5C4659F5B295E033 CRC64;
MRIPRIYHPE PLTSHSHIAL CEDAANHIGR VLRMGPGQAL QLFDGSNQVF DAEITSASKK
SVEVKVLEGQ IDDRESPLHI HLGQVMSRGE KMEFTIQKSI ELGVSLITPL FSERCGVKLD
SERLNKKLQQ WQKIAIAACE QCGRNRVPEI RPAMDLEAWC AEQDEGLKLN LHPRASNSIN
TLPLPVERVR LLIGPEGGLS ADEIAMTARY QFTDILLGPR VLRTETTALT AITALQVRFG
DLG
