RSMH_STRPN
ID RSMH_STRPN Reviewed; 316 AA.
AC P0CB58; P72491; Q97SK1; Q9R8Q8;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 63.
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=SP_0334;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Cp5500;
RA Palmen R., Mallet O., Berroy P.J.M., Trombe M.C.;
RT "Sequence of a genetic region of Streptococcus pneumoniae similar to the
RT dcw region in Escherichia coli, Bacillus subtilis and Haemophilus
RT influenzae.";
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
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; Z79691; CAB01927.1; -; Genomic_DNA.
DR EMBL; AE005672; AAK74509.1; -; Genomic_DNA.
DR PIR; D95039; D95039.
DR PIR; F97909; F97909.
DR RefSeq; WP_000159382.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; P0CB58; -.
DR SMR; P0CB58; -.
DR STRING; 170187.SP_0334; -.
DR EnsemblBacteria; AAK74509; AAK74509; SP_0334.
DR KEGG; spn:SP_0334; -.
DR eggNOG; COG0275; Bacteria.
DR OMA; NPAKRTF; -.
DR PhylomeDB; P0CB58; -.
DR BioCyc; SPNE170187:G1FZB-343-MON; -.
DR Proteomes; UP000000585; 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_0000108719"
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"
FT CONFLICT 24
FT /note="D -> E (in Ref. 1; CAB01927)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="C -> R (in Ref. 1; CAB01927)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="N -> H (in Ref. 1; CAB01927)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 316 AA; 35975 MW; E04066B2C2EFE020 CRC64;
MTKEFHHVTV LLHETIDMLD VKPDGIYVDA TLGGAGHSEY LLSKLSEKGH LYAFDQDQNA
IDNAQKRLAP YIEKGMVTFI KDNFRHLQAC LREAGVQEID GICYDLGVSS PQLDQRERGF
SYKKDAPLDM RMNQDASLTA YEVVNNYDYH DLVRIFFKYG EDKFSKQIAR KIEQAREVKP
IETTTELAEI IKLVKPAKEL KKKGHPAKQI FQAIRIEVND ELGAADESIQ QAMDMLALDG
RISVITFHSL EDRLTKQLFK EASTVEVPKG LPFIPDDLKP KMELVSRKPI LPSAEELEAN
NRSHSAKLRV VRKIHK
