RSMC_ECOLI
ID RSMC_ECOLI Reviewed; 343 AA.
AC P39406; Q2M5U7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase C;
DE EC=2.1.1.172 {ECO:0000269|PubMed:9873033};
DE AltName: Full=16S rRNA m2G1207 methyltransferase;
DE AltName: Full=rRNA (guanine-N(2)-)-methyltransferase RsmC;
GN Name=rsmC; Synonyms=yjjT; OrderedLocusNames=b4371, JW4333;
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=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
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 [3]
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 [4]
RP PROTEIN SEQUENCE OF 2-20, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9873033; DOI=10.1074/jbc.274.2.924;
RA Tscherne J.S., Nurse K., Popienick P., Ofengand J.;
RT "Purification, cloning, and characterization of the 16S RNA m2G1207
RT methyltransferase from Escherichia coli.";
RL J. Biol. Chem. 274:924-929(1999).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), MUTAGENESIS OF LYS-86; LYS-88;
RP ASP-202; ASP-227 AND ASN-268, AND SUBUNIT.
RX PubMed=17576679; DOI=10.1093/nar/gkm411;
RA Sunita S., Purta E., Durawa M., Tkaczuk K.L., Swaathi J., Bujnicki J.M.,
RA Sivaraman J.;
RT "Functional specialization of domains tandemly duplicated within 16S rRNA
RT methyltransferase RsmC.";
RL Nucleic Acids Res. 35:4264-4274(2007).
CC -!- FUNCTION: Specifically methylates the guanine in position 1207 of 16S
CC rRNA in the 30S particle. {ECO:0000269|PubMed:9873033}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(1207) in 16S rRNA + S-adenosyl-L-methionine = H(+) +
CC N(2)-methylguanosine(1207) in 16S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42736, Rhea:RHEA-COMP:10213, Rhea:RHEA-COMP:10214,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; EC=2.1.1.172;
CC Evidence={ECO:0000269|PubMed:9873033};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42737;
CC Evidence={ECO:0000269|PubMed:9873033};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17576679}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmC family.
CC {ECO:0000305}.
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DR EMBL; U14003; AAA97267.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77324.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78359.1; -; Genomic_DNA.
DR PIR; S56595; S56595.
DR RefSeq; NP_418788.1; NC_000913.3.
DR RefSeq; WP_001272330.1; NZ_LN832404.1.
DR PDB; 2PJD; X-ray; 2.10 A; A=1-343.
DR PDBsum; 2PJD; -.
DR AlphaFoldDB; P39406; -.
DR SMR; P39406; -.
DR BioGRID; 4262778; 51.
DR DIP; DIP-10804N; -.
DR IntAct; P39406; 15.
DR STRING; 511145.b4371; -.
DR jPOST; P39406; -.
DR PaxDb; P39406; -.
DR PRIDE; P39406; -.
DR EnsemblBacteria; AAC77324; AAC77324; b4371.
DR EnsemblBacteria; BAE78359; BAE78359; BAE78359.
DR GeneID; 948892; -.
DR KEGG; ecj:JW4333; -.
DR KEGG; eco:b4371; -.
DR PATRIC; fig|1411691.4.peg.2317; -.
DR EchoBASE; EB2481; -.
DR eggNOG; COG2813; Bacteria.
DR HOGENOM; CLU_049581_0_1_6; -.
DR InParanoid; P39406; -.
DR OMA; RHCQLWQ; -.
DR PhylomeDB; P39406; -.
DR BioCyc; EcoCyc:G7950-MON; -.
DR BioCyc; MetaCyc:G7950-MON; -.
DR BRENDA; 2.1.1.172; 2026.
DR EvolutionaryTrace; P39406; -.
DR PRO; PR:P39406; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IC:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0052914; F:16S rRNA (guanine(1207)-N(2))-methyltransferase activity; IDA:EcoCyc.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008990; F:rRNA (guanine-N2-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0034337; P:RNA folding; IDA:EcoCyc.
DR GO; GO:0070475; P:rRNA base methylation; IMP:EcoCyc.
DR GO; GO:0031167; P:rRNA methylation; IDA:UniProtKB.
DR Gene3D; 3.40.50.150; -; 2.
DR HAMAP; MF_01862; 16SrRNA_methyltr_C; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR013675; Mtase_sm_N.
DR InterPro; IPR023543; rRNA_ssu_MeTfrase_C.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR007848; Small_mtfrase_dom.
DR Pfam; PF05175; MTS; 1.
DR Pfam; PF08468; MTS_N; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Magnesium;
KW Methyltransferase; Reference proteome; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9873033"
FT CHAIN 2..343
FT /note="Ribosomal RNA small subunit methyltransferase C"
FT /id="PRO_0000097490"
FT MUTAGEN 86
FT /note="K->S: Reduces activity by 84%; when associated with
FT S-88."
FT /evidence="ECO:0000269|PubMed:17576679"
FT MUTAGEN 88
FT /note="K->S: Reduces activity by 84%; when associated with
FT S-86."
FT /evidence="ECO:0000269|PubMed:17576679"
FT MUTAGEN 202
FT /note="D->A: Abolishes affinity for S-adenosyl-L-
FT methionine. Loss of activity."
FT /evidence="ECO:0000269|PubMed:17576679"
FT MUTAGEN 227
FT /note="D->A: Strongly reduces affinity for S-adenosyl-L-
FT methionine. Reduces activity by 87%."
FT /evidence="ECO:0000269|PubMed:17576679"
FT MUTAGEN 268
FT /note="N->A: Reduces affinity for S-adenosyl-L-methionine.
FT Reduces activity by 80%."
FT /evidence="ECO:0000269|PubMed:17576679"
FT HELIX 6..12
FT /evidence="ECO:0007829|PDB:2PJD"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:2PJD"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:2PJD"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:2PJD"
FT STRAND 40..48
FT /evidence="ECO:0007829|PDB:2PJD"
FT HELIX 49..59
FT /evidence="ECO:0007829|PDB:2PJD"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:2PJD"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:2PJD"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:2PJD"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:2PJD"
FT HELIX 88..99
FT /evidence="ECO:0007829|PDB:2PJD"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:2PJD"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:2PJD"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:2PJD"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:2PJD"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:2PJD"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:2PJD"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:2PJD"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:2PJD"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:2PJD"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:2PJD"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:2PJD"
FT HELIX 183..191
FT /evidence="ECO:0007829|PDB:2PJD"
FT HELIX 209..217
FT /evidence="ECO:0007829|PDB:2PJD"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:2PJD"
FT HELIX 230..242
FT /evidence="ECO:0007829|PDB:2PJD"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:2PJD"
FT TURN 254..257
FT /evidence="ECO:0007829|PDB:2PJD"
FT STRAND 262..267
FT /evidence="ECO:0007829|PDB:2PJD"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:2PJD"
FT HELIX 276..289
FT /evidence="ECO:0007829|PDB:2PJD"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:2PJD"
FT STRAND 293..304
FT /evidence="ECO:0007829|PDB:2PJD"
FT HELIX 309..317
FT /evidence="ECO:0007829|PDB:2PJD"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:2PJD"
FT STRAND 327..335
FT /evidence="ECO:0007829|PDB:2PJD"
SQ SEQUENCE 343 AA; 37625 MW; 81E190CB86E4BAC2 CRC64;
MSAFTPASEV LLRHSDDFEQ SRILFAGDLQ DDLPARLDTA ASRAHTQQFH HWQVLSRQMG
DNARFSLVAT ADDVADCDTL IYYWPKNKPE AQFQLMNLLS LLPVGTDIFV VGENRSGVRS
AEQMLADYAP LNKVDSARRC GLYFGRLEKQ PVFDAEKFWG EYSVDGLTVK TLPGVFSRDG
LDVGSQLLLS TLTPHTKGKV LDVGCGAGVL SVAFARHSPK IRLTLCDVSA PAVEASRATL
AANGVEGEVF ASNVFSEVKG RFDMIISNPP FHDGMQTSLD AAQTLIRGAV RHLNSGGELR
IVANAFLPYP DVLDETFGFH EVIAQTGRFK VYRAIMTRQA KKG
