RSMH_STRDG
ID RSMH_STRDG Reviewed; 316 AA.
AC C5WIJ4;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 70.
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=SDEG_1726;
OS Streptococcus dysgalactiae subsp. equisimilis (strain GGS_124).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=486410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GGS_124;
RX PubMed=21223537; DOI=10.1186/1471-2164-12-17;
RA Shimomura Y., Okumura K., Murayama S.Y., Yagi J., Ubukata K., Kirikae T.,
RA Miyoshi-Akiyama T.;
RT "Complete genome sequencing and analysis of a Lancefield group G
RT Streptococcus dysgalactiae subsp. equisimilis strain causing streptococcal
RT toxic shock syndrome (STSS).";
RL BMC Genomics 12:17-17(2011).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAH82209.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP010935; BAH82209.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; C5WIJ4; -.
DR SMR; C5WIJ4; -.
DR EnsemblBacteria; BAH82209; BAH82209; SDEG_1726.
DR KEGG; sds:SDEG_1726; -.
DR HOGENOM; CLU_038422_2_0_9; -.
DR OMA; NPAKRTF; -.
DR Proteomes; UP000002732; 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..316
FT /note="Ribosomal RNA small subunit methyltransferase H"
FT /id="PRO_0000387144"
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 84
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT BINDING 105
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT BINDING 112
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
SQ SEQUENCE 316 AA; 35652 MW; D9E575D5EAC7370F CRC64;
MTKEFHHVTV LLHETVDMLD IKPNGIYVDA TLGGSGHSAY LLSKLSEQGH LYCFDQDQKA
IDNAQVTLKS YIDKGQVTFI KDNFRHLKAR LTALGVDEID GILYDLGVSS PQLDERERGF
SYNQDAPLDM RMDRQAPLTA YDVVNTYPFN DLVKIFFKYG EDKFSKQIAR KIEQARAIKP
IETTTELAEL IKAAKPAKEL KKKGHPAKQI FQAIRIEVND ELGAADESIQ DAMELLALDG
RISVITFHSL EDRLTKQLFK EASTVDVPKG LPFIPEDMKP TFELVSRKPI LPSQEELAAN
NRAHSAKLRV AKKIRK