RSMH_ENTFA
ID RSMH_ENTFA Reviewed; 318 AA.
AC O07104;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 3.
DT 03-AUG-2022, entry version 129.
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=EF_0989;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A24836;
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=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
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=AAC45631.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAO80795.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U94707; AAC45631.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE016830; AAO80795.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_814725.1; NC_004668.1.
DR RefSeq; WP_002355891.1; NC_004668.1.
DR AlphaFoldDB; O07104; -.
DR SMR; O07104; -.
DR STRING; 226185.EF_0989; -.
DR EnsemblBacteria; AAO80795; AAO80795; EF_0989.
DR GeneID; 60893376; -.
DR KEGG; efa:EF0989; -.
DR PATRIC; fig|226185.45.peg.3195; -.
DR eggNOG; COG0275; Bacteria.
DR HOGENOM; CLU_038422_2_0_9; -.
DR OMA; NPAKRTF; -.
DR Proteomes; UP000001415; 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; Reference proteome; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..318
FT /note="Ribosomal RNA small subunit methyltransferase H"
FT /id="PRO_0000108625"
FT REGION 294..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 2
FT /note="T -> I (in Ref. 1; AAC45631)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="L -> F (in Ref. 1; AAC45631)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 318 AA; 36162 MW; 408FDCA81CFBA5B7 CRC64;
MTEEFRHYTV LLKETVDGLQ VKPDGVYVDC TLGGAGHSEY LLTQLNEHGH LYAFDQDQKA
LAHAKTRLQK YVDKGQVTFI KSNFRNIKEE LAEHGVFHVD GILYDLGVSS PQLDEAERGF
SYHQDAPLDM RMDQDAPLTA REVVNTYSYS ELVKIFFRYG EEKFSKQIAR EIERVREKQP
IETTGELVEI IKTAIPAPAR RKGGHPAKRI FQAIRIAVND ELGAVEESLE QAIDLLAKNG
RISVITFHSL EDRIVKTMFK EYSTVQDLPP GIPVVPEEFQ PELKVITRKP ILPSDSELSE
NNRSRSAKLR IAEKIKSR
