ID   RSMH_HELPB              Reviewed;         308 AA.
AC   C7BZ94;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=HELPY_0659;
OS   Helicobacter pylori (strain B38).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=592205;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B38;
RX   PubMed=20537153; DOI=10.1186/1471-2164-11-368;
RA   Thiberge J.M., Boursaux-Eude C., Lehours P., Dillies M.A., Creno S.,
RA   Coppee J.Y., Rouy Z., Lajus A., Ma L., Burucoa C., Ruskone-Foumestraux A.,
RA   Courillon-Mallet A., De Reuse H., Boneca I.G., Lamarque D., Megraud F.,
RA   Delchier J.C., Medigue C., Bouchier C., Labigne A., Raymond J.;
RT   "From array-based hybridization of Helicobacter pylori isolates to the
RT   complete genome sequence of an isolate associated with MALT lymphoma.";
RL   BMC Genomics 11:368-368(2010).
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; FM991728; CAX29192.1; -; Genomic_DNA.
DR   RefSeq; WP_001155546.1; NC_012973.1.
DR   AlphaFoldDB; C7BZ94; -.
DR   SMR; C7BZ94; -.
DR   EnsemblBacteria; CAX29192; CAX29192; HELPY_0659.
DR   KEGG; hpb:HELPY_0659; -.
DR   HOGENOM; CLU_038422_3_0_7; -.
DR   OMA; NPAKRTF; -.
DR   OrthoDB; 1272633at2; -.
DR   BioCyc; HPYL592205:HELPY_RS03200-MON; -.
DR   Proteomes; UP000000313; 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..308
FT                   /note="Ribosomal RNA small subunit methyltransferase H"
FT                   /id="PRO_0000386926"
FT   BINDING         36..38
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         86
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         103
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         110
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
SQ   SEQUENCE   308 AA;  34973 MW;  49F442D1C061E4BE CRC64;
     MQEIENLHQS VLLQEVLQAF TPLEEGVLID CTLGLGGHSK ALLSQKPHLK LIGIDKDKFA
     QEIAKERLKA FEGRYNLLSG GFAKRFKEAL ETHNKEIKGV LVDLGVSSLQ LDDDDRGFNF
     HSHALDMRMD LKSDLNAQKV INSYPVIALE KIFRDYGEIK EYKKIAHKIA ERRTKKPFKD
     AKDLSEFLSS FSKNKKIHPA TLVFQAVRIE VNSELEELKE FLQCARNLKG AILCVISFHS
     LEDGLVKNAF KDYAKNCICD PLSFKCACSN NHALGEILTK KPITPSPEEI KNNRRSRSAK
     MRVFKFKP