RSMH_ECOLI
ID RSMH_ECOLI Reviewed; 313 AA.
AC P60390; P18595;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase H;
DE EC=2.1.1.199;
DE AltName: Full=16S rRNA m(4)C1402 methyltransferase;
DE AltName: Full=rRNA (cytosine-N(4)-)-methyltransferase RsmH;
GN Name=rsmH; Synonyms=mraW, yabC; OrderedLocusNames=b0082, JW0080;
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=2187182; DOI=10.1093/nar/18.9.2813;
RA Gomez M.J., Fluoret B., van Heijenoort J., Ayala J.A.;
RT "Nucleotide sequence of the regulatory region of the gene pbpB of
RT Escherichia coli.";
RL Nucleic Acids Res. 18:2813-2813(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 232-313.
RC STRAIN=K12;
RX PubMed=6350821; DOI=10.1007/bf00330881;
RA Nakamura M., Maruyama I.N., Soma M., Kato J., Suzuki H., Horota Y.;
RT "On the process of cellular division in Escherichia coli: nucleotide
RT sequence of the gene for penicillin-binding protein 3.";
RL Mol. Gen. Genet. 191:1-9(1983).
RN [6]
RP PROTEIN SEQUENCE OF 1-16, FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=10572301; DOI=10.1016/s0300-9084(99)00208-4;
RA Carrion M., Gomez M.J., Merchante-Schubert R., Dongarra S., Ayala J.A.;
RT "mraW, an essential gene at the dcw cluster of Escherichia coli codes for a
RT cytoplasmic protein with methyltransferase activity.";
RL Biochimie 81:879-888(1999).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=B / BL21;
RX PubMed=10493123;
RX DOI=10.1002/(sici)1522-2683(19990801)20:11<2181::aid-elps2181>3.0.co;2-q;
RA Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
RT "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite
RT chromatography.";
RL Electrophoresis 20:2181-2195(1999).
RN [8]
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: Specifically methylates the N4 position of cytidine in
CC position 1402 (C1402) of 16S rRNA. In vitro, active on the assembled
CC 30S subunit, but not naked 16S rRNA or 70S ribosomes.
CC {ECO:0000269|PubMed:10572301, ECO:0000269|PubMed:19965768}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) +
CC N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42928, Rhea:RHEA-COMP:10286, Rhea:RHEA-COMP:10287,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74506, ChEBI:CHEBI:82748; EC=2.1.1.199;
CC Evidence={ECO:0000269|PubMed:19965768};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10572301}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmH family.
CC {ECO:0000305}.
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DR EMBL; X52063; CAA36283.1; -; Genomic_DNA.
DR EMBL; X55034; CAA38859.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73193.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96650.1; -; Genomic_DNA.
DR EMBL; K00137; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; JH0092; QQECFT.
DR RefSeq; NP_414624.1; NC_000913.3.
DR RefSeq; WP_000970479.1; NZ_STEB01000010.1.
DR PDB; 3TKA; X-ray; 2.25 A; A=1-313.
DR PDBsum; 3TKA; -.
DR AlphaFoldDB; P60390; -.
DR SMR; P60390; -.
DR BioGRID; 4261639; 47.
DR BioGRID; 849207; 1.
DR DIP; DIP-35840N; -.
DR IntAct; P60390; 7.
DR STRING; 511145.b0082; -.
DR jPOST; P60390; -.
DR PaxDb; P60390; -.
DR PRIDE; P60390; -.
DR EnsemblBacteria; AAC73193; AAC73193; b0082.
DR EnsemblBacteria; BAB96650; BAB96650; BAB96650.
DR GeneID; 67416155; -.
DR GeneID; 944806; -.
DR KEGG; ecj:JW0080; -.
DR KEGG; eco:b0082; -.
DR PATRIC; fig|1411691.4.peg.2198; -.
DR EchoBASE; EB1077; -.
DR eggNOG; COG0275; Bacteria.
DR HOGENOM; CLU_038422_2_0_6; -.
DR InParanoid; P60390; -.
DR OMA; NPAKRTF; -.
DR PhylomeDB; P60390; -.
DR BioCyc; EcoCyc:EG11085-MON; -.
DR BioCyc; MetaCyc:EG11085-MON; -.
DR BRENDA; 2.1.1.199; 2026.
DR PRO; PR:P60390; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0071424; F:rRNA (cytosine-N4-)-methyltransferase activity; IDA:EcoCyc.
DR GO; GO:0070475; P:rRNA base methylation; IMP:EcoCyc.
DR Gene3D; 1.10.150.170; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01007; 16SrRNA_methyltr_H; 1.
DR InterPro; IPR002903; RsmH.
DR InterPro; IPR023397; SAM-dep_MeTrfase_MraW_recog.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11265; PTHR11265; 1.
DR Pfam; PF01795; Methyltransf_5; 1.
DR PIRSF; PIRSF004486; MraW; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF81799; SSF81799; 1.
DR TIGRFAMs; TIGR00006; TIGR00006; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Methyltransferase;
KW Reference proteome; rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..313
FT /note="Ribosomal RNA small subunit methyltransferase H"
FT /id="PRO_0000108620"
FT BINDING 35..37
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:3TKA"
FT HELIX 13..18
FT /evidence="ECO:0007829|PDB:3TKA"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:3TKA"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:3TKA"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:3TKA"
FT HELIX 58..64
FT /evidence="ECO:0007829|PDB:3TKA"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:3TKA"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:3TKA"
FT HELIX 82..88
FT /evidence="ECO:0007829|PDB:3TKA"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:3TKA"
FT HELIX 106..110
FT /evidence="ECO:0007829|PDB:3TKA"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:3TKA"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:3TKA"
FT HELIX 136..142
FT /evidence="ECO:0007829|PDB:3TKA"
FT HELIX 145..156
FT /evidence="ECO:0007829|PDB:3TKA"
FT HELIX 161..174
FT /evidence="ECO:0007829|PDB:3TKA"
FT HELIX 180..190
FT /evidence="ECO:0007829|PDB:3TKA"
FT HELIX 202..213
FT /evidence="ECO:0007829|PDB:3TKA"
FT HELIX 215..229
FT /evidence="ECO:0007829|PDB:3TKA"
FT STRAND 230..242
FT /evidence="ECO:0007829|PDB:3TKA"
FT HELIX 243..255
FT /evidence="ECO:0007829|PDB:3TKA"
FT STRAND 281..287
FT /evidence="ECO:0007829|PDB:3TKA"
FT HELIX 291..296
FT /evidence="ECO:0007829|PDB:3TKA"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:3TKA"
FT STRAND 304..310
FT /evidence="ECO:0007829|PDB:3TKA"
SQ SEQUENCE 313 AA; 34878 MW; 43174C907A36ECC1 CRC64;
MMENYKHTTV LLDEAVNGLN IRPDGIYIDG TFGRGGHSRL ILSQLGEEGR LLAIDRDPQA
IAVAKTIDDP RFSIIHGPFS ALGEYVAERD LIGKIDGILL DLGVSSPQLD DAERGFSFMR
DGPLDMRMDP TRGQSAAEWL QTAEEADIAW VLKTYGEERF AKRIARAIVE RNREQPMTRT
KELAEVVAAA TPVKDKFKHP ATRTFQAVRI WVNSELEEIE QALKSSLNVL APGGRLSIIS
FHSLEDRIVK RFMRENSRGP QVPAGLPMTE EQLKKLGGRQ LRALGKLMPG EEEVAENPRA
RSSVLRIAER TNA
