RSMH_ECOBD
ID RSMH_ECOBD Reviewed; 313 AA.
AC C5W331; C6EAX3;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase H {ECO:0000255|HAMAP-Rule:MF_01007};
DE EC=2.1.1.199 {ECO:0000255|HAMAP-Rule:MF_01007};
DE AltName: Full=16S rRNA m(4)C1402 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01007};
DE AltName: Full=rRNA (cytosine-N(4)-)-methyltransferase RsmH {ECO:0000255|HAMAP-Rule:MF_01007};
GN Name=rsmH {ECO:0000255|HAMAP-Rule:MF_01007}; Synonyms=mraW;
GN OrderedLocusNames=ECBD_3535, ECD_00083, B21_00082;
OS Escherichia coli (strain B / BL21-DE3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=469008;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B / BL21-DE3;
RA Leparc G., Striedner G., Bayer K., Kreil D., Krempl P.M.;
RT "Sequencing and gene expression analysis of Escherichia coli BL21.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B / BL21-DE3;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., Rubin E.;
RT "Complete sequence of Escherichia coli BL21(DE3).";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B / BL21-DE3;
RX PubMed=19786035; DOI=10.1016/j.jmb.2009.09.052;
RA Jeong H., Barbe V., Lee C.H., Vallenet D., Yu D.S., Choi S.H., Couloux A.,
RA Lee S.W., Yoon S.H., Cattolico L., Hur C.G., Park H.S., Segurens B.,
RA Kim S.C., Oh T.K., Lenski R.E., Studier F.W., Daegelen P., Kim J.F.;
RT "Genome sequences of Escherichia coli B strains REL606 and BL21(DE3).";
RL J. Mol. Biol. 394:644-652(2009).
CC -!- FUNCTION: Specifically methylates the N4 position of cytidine in
CC position 1402 (C1402) of 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_01007}.
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:0000255|HAMAP-Rule:MF_01007};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01007}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmH family.
CC {ECO:0000255|HAMAP-Rule:MF_01007}.
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DR EMBL; AM946981; CAQ30599.1; -; Genomic_DNA.
DR EMBL; CP001665; ACT30534.1; -; Genomic_DNA.
DR EMBL; CP001509; ACT41984.1; -; Genomic_DNA.
DR RefSeq; WP_000970479.1; NZ_CP053602.1.
DR AlphaFoldDB; C5W331; -.
DR SMR; C5W331; -.
DR STRING; 469008.B21_00082; -.
DR GeneID; 67416155; -.
DR KEGG; ebd:ECBD_3535; -.
DR KEGG; ebe:B21_00082; -.
DR KEGG; ebl:ECD_00083; -.
DR PATRIC; fig|469008.15.peg.81; -.
DR eggNOG; COG0275; Bacteria.
DR HOGENOM; CLU_038422_2_0_6; -.
DR OMA; NPAKRTF; -.
DR Proteomes; UP000002032; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0071424; F:rRNA (cytosine-N4-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070475; P:rRNA base methylation; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; rRNA processing; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..313
FT /note="Ribosomal RNA small subunit methyltransferase H"
FT /id="PRO_0000386869"
FT BINDING 35..37
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT BINDING 55
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT BINDING 79
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT BINDING 101
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT BINDING 108
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
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
