RSMD_ECOLI
ID RSMD_ECOLI Reviewed; 198 AA.
AC P0ADX9; P10120; Q2M7C8;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase D;
DE EC=2.1.1.171 {ECO:0000269|PubMed:17189261};
DE AltName: Full=16S rRNA m2G966 methyltransferase {ECO:0000303|PubMed:17189261};
DE AltName: Full=rRNA (guanine-N(2)-)-methyltransferase;
GN Name=rsmD; Synonyms=yhhF; OrderedLocusNames=b3465, JW3430;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3025556; DOI=10.1007/bf02428043;
RA Gill D.R., Hatfull G.F., Salmond G.P.C.;
RT "A new cell division operon in Escherichia coli.";
RL Mol. Gen. Genet. 205:134-145(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [3]
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 [4]
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 [5]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS), FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17189261; DOI=10.1074/jbc.m608214200;
RA Lesnyak D.V., Osipiuk J., Skarina T., Sergiev P.V., Bogdanov A.A.,
RA Edwards A., Savchenko A., Joachimiak A., Dontsova O.A.;
RT "Methyltransferase that modifies guanine 966 of the 16 S rRNA: functional
RT identification and tertiary structure.";
RL J. Biol. Chem. 282:5880-5887(2007).
CC -!- FUNCTION: Specifically methylates the guanine in position 966 of 16S
CC rRNA in the assembled 30S particle. {ECO:0000269|PubMed:17189261}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(966) in 16S rRNA + S-adenosyl-L-methionine = H(+) +
CC N(2)-methylguanosine(966) in 16S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:23548, Rhea:RHEA-COMP:10211, Rhea:RHEA-COMP:10212,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; EC=2.1.1.171;
CC Evidence={ECO:0000269|PubMed:17189261};
CC -!- INTERACTION:
CC P0ADX9; P0A6Y8: dnaK; NbExp=2; IntAct=EBI-561207, EBI-542092;
CC P0ADX9; P0CE47: tufA; NbExp=2; IntAct=EBI-561207, EBI-301077;
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmD family.
CC {ECO:0000305}.
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DR EMBL; X04398; CAA27983.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18440.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76490.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77828.1; -; Genomic_DNA.
DR PIR; S03129; QQECX3.
DR RefSeq; NP_417922.1; NC_000913.3.
DR RefSeq; WP_000743193.1; NZ_STEB01000004.1.
DR PDB; 2FPO; X-ray; 2.05 A; A/B/C/D/E/F=1-198.
DR PDBsum; 2FPO; -.
DR AlphaFoldDB; P0ADX9; -.
DR SMR; P0ADX9; -.
DR BioGRID; 4262500; 62.
DR DIP; DIP-48275N; -.
DR IntAct; P0ADX9; 6.
DR STRING; 511145.b3465; -.
DR SWISS-2DPAGE; P0ADX9; -.
DR jPOST; P0ADX9; -.
DR PaxDb; P0ADX9; -.
DR PRIDE; P0ADX9; -.
DR EnsemblBacteria; AAC76490; AAC76490; b3465.
DR EnsemblBacteria; BAE77828; BAE77828; BAE77828.
DR GeneID; 66672651; -.
DR GeneID; 947977; -.
DR KEGG; ecj:JW3430; -.
DR KEGG; eco:b3465; -.
DR PATRIC; fig|511145.12.peg.3564; -.
DR EchoBASE; EB0339; -.
DR eggNOG; COG0742; Bacteria.
DR HOGENOM; CLU_075826_2_2_6; -.
DR InParanoid; P0ADX9; -.
DR OMA; FNWLMPY; -.
DR PhylomeDB; P0ADX9; -.
DR BioCyc; EcoCyc:EG10343-MON; -.
DR BioCyc; MetaCyc:EG10343-MON; -.
DR BRENDA; 2.1.1.171; 2026.
DR EvolutionaryTrace; P0ADX9; -.
DR PRO; PR:P0ADX9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0052913; F:16S rRNA (guanine(966)-N(2))-methyltransferase activity; IDA:EcoCyc.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0070475; P:rRNA base methylation; IMP:EcoCyc.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR004398; RNA_MeTrfase_RsmD.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PIRSF; PIRSF004553; CHP00095; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00095; TIGR00095; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Methyltransferase; Reference proteome; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..198
FT /note="Ribosomal RNA small subunit methyltransferase D"
FT /id="PRO_0000169548"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:2FPO"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:2FPO"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:2FPO"
FT HELIX 37..51
FT /evidence="ECO:0007829|PDB:2FPO"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:2FPO"
FT HELIX 65..72
FT /evidence="ECO:0007829|PDB:2FPO"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:2FPO"
FT HELIX 85..97
FT /evidence="ECO:0007829|PDB:2FPO"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:2FPO"
FT HELIX 110..114
FT /evidence="ECO:0007829|PDB:2FPO"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:2FPO"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:2FPO"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:2FPO"
FT HELIX 135..144
FT /evidence="ECO:0007829|PDB:2FPO"
FT STRAND 148..159
FT /evidence="ECO:0007829|PDB:2FPO"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:2FPO"
FT STRAND 171..179
FT /evidence="ECO:0007829|PDB:2FPO"
FT STRAND 182..189
FT /evidence="ECO:0007829|PDB:2FPO"
SQ SEQUENCE 198 AA; 21678 MW; 04FB9D9DAF972605 CRC64;
MKKPNHSGSG QIRIIGGQWR GRKLPVPDSP GLRPTTDRVR ETLFNWLAPV IVDAQCLDCF
AGSGALGLEA LSRYAAGATL IEMDRAVSQQ LIKNLATLKA GNARVVNSNA MSFLAQKGTP
HNIVFVDPPF RRGLLEETIN LLEDNGWLAD EALIYVESEV ENGLPTVPAN WSLHREKVAG
QVAYRLYQRE AQGESDAD
