ID   RSMH_STRS4              Reviewed;         316 AA.
AC   C6GW75;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=SSUBM407_1624;
OS   Streptococcus suis (strain BM407).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=568814;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BM407;
RX   PubMed=19603075; DOI=10.1371/journal.pone.0006072;
RA   Holden M.T.G., Hauser H., Sanders M., Ngo T.H., Cherevach I., Cronin A.,
RA   Goodhead I., Mungall K., Quail M.A., Price C., Rabbinowitsch E., Sharp S.,
RA   Croucher N.J., Chieu T.B., Mai N.T.H., Diep T.S., Chinh N.T., Kehoe M.,
RA   Leigh J.A., Ward P.N., Dowson C.G., Whatmore A.M., Chanter N., Iversen P.,
RA   Gottschalk M., Slater J.D., Smith H.E., Spratt B.G., Xu J., Ye C.,
RA   Bentley S., Barrell B.G., Schultsz C., Maskell D.J., Parkhill J.;
RT   "Rapid evolution of virulence and drug resistance in the emerging zoonotic
RT   pathogen Streptococcus suis.";
RL   PLoS ONE 4:E6072-E6072(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FM252032; CAZ56480.1; -; Genomic_DNA.
DR   RefSeq; WP_002937995.1; NC_012926.1.
DR   RefSeq; YP_003029321.1; NC_012926.1.
DR   AlphaFoldDB; C6GW75; -.
DR   SMR; C6GW75; -.
DR   EnsemblBacteria; CAZ56480; CAZ56480; SSUBM407_1624.
DR   GeneID; 8153161; -.
DR   KEGG; ssb:SSUBM407_1624; -.
DR   PATRIC; fig|568814.3.peg.1661; -.
DR   HOGENOM; CLU_038422_2_0_9; -.
DR   OMA; NPAKRTF; -.
DR   Proteomes; UP000009077; 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_0000387167"
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;  35731 MW;  84FF39B1BAE6DF02 CRC64;
     MTKEFNHTTV LLHETVDMLD IKPNGIYVDA TLGGAGHSEY LLSQLTDGGH LYAFDQDQTA
     IDHAHIRLAS YIEKGQVTFI RDNFRNLKTR LAELGVTEID GICYDLGVSS PQLDERERGF
     SYKQDAPLDM RMNREGHLTA YDVVNNYDYH DLVRIFFKYG EDKFSKQIAR KIEQARAVKP
     IETTTELAEL IKSAKPAKEL KKKGHPAKQI FQAIRIEVND ELGAADESIQ QAIDLLALDG
     RISVITFHSL EDRLTKQLFK EASTIDVPKG LPFIPDDLKA PLELVNRKPI LPSQEELEAN
     NRAHSAKLRV AKKVHK