ID   RSMH_STAA8              Reviewed;         311 AA.
AC   P60393; O07320; Q2FZ96;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-FEB-2004, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=SAOUHSC_01143;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9287029; DOI=10.1128/jb.179.17.5632-5635.1997;
RA   Pucci M.J., Thanassi J.A., Discotto L.F., Kessler R.E., Dougherty T.J.;
RT   "Identification and characterization of cell wall-cell division gene
RT   clusters in pathogenic Gram-positive cocci.";
RL   J. Bacteriol. 179:5632-5635(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 247-311.
RX   PubMed=9573165; DOI=10.1128/jb.180.10.2759-2765.1998;
RA   Wada A., Watanabe H.;
RT   "Penicillin-binding protein 1 of Staphylococcus aureus is essential for
RT   growth.";
RL   J. Bacteriol. 180:2759-2765(1998).
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=ABD30253.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U94706; AAC45622.1; -; Genomic_DNA.
DR   EMBL; CP000253; ABD30253.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AB007500; BAA22552.1; -; Genomic_DNA.
DR   RefSeq; WP_000468384.1; NZ_LS483365.1.
DR   RefSeq; YP_499685.1; NC_007795.1.
DR   AlphaFoldDB; P60393; -.
DR   SMR; P60393; -.
DR   STRING; 1280.SAXN108_1177; -.
DR   EnsemblBacteria; ABD30253; ABD30253; SAOUHSC_01143.
DR   GeneID; 3920703; -.
DR   KEGG; sao:SAOUHSC_01143; -.
DR   PATRIC; fig|93061.5.peg.1048; -.
DR   eggNOG; COG0275; Bacteria.
DR   HOGENOM; CLU_038422_2_0_9; -.
DR   PRO; PR:P60393; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0071424; F:rRNA (cytosine-N4-)-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central.
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; Reference proteome; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..311
FT                   /note="Ribosomal RNA small subunit methyltransferase H"
FT                   /id="PRO_0000108710"
FT   BINDING         32..34
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         52
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         100
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         107
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
SQ   SEQUENCE   311 AA;  35682 MW;  035B40F52DA1941D CRC64;
     MFHHISVMLN ETIDYLNVKE NGVYIDCTLG GAGHALYLLN QLNDDGRLIA IDQDQTAIDN
     AKEVLKDHLH KVTFVHSNFR ELTQILKDLN IEKVDGIYYD LGVSSPQLDI PERGFSYHHD
     ATLDMRMDQT QELTAYEIVN NWSYEALVKI FYRYGEEKFS KQIARRIEAH REQQPITTTL
     ELVDIIKEGI PAKARRKGGH PAKRVFQALR IAVNDELSAF EDSIEQAIEL VKVDGRISVI
     TFHSLEDRLC KQVFQEYEKG PEVPRGLPVI PEAYTPKLKR VNRKPITATE EDLDDNNRAR
     SAKLRVAEIL K