ID RSMA_HELPY Reviewed; 271 AA. AC O25972; DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 27-MAR-2024, entry version 126. DE RecName: Full=Ribosomal RNA small subunit methyltransferase A {ECO:0000255|HAMAP-Rule:MF_00607}; DE EC=2.1.1.182 {ECO:0000255|HAMAP-Rule:MF_00607}; DE AltName: Full=16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase {ECO:0000255|HAMAP-Rule:MF_00607}; DE AltName: Full=16S rRNA dimethyladenosine transferase {ECO:0000255|HAMAP-Rule:MF_00607}; DE AltName: Full=16S rRNA dimethylase {ECO:0000255|HAMAP-Rule:MF_00607}; DE AltName: Full=S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase {ECO:0000255|HAMAP-Rule:MF_00607}; GN Name=rsmA {ECO:0000255|HAMAP-Rule:MF_00607}; GN Synonyms=ksgA {ECO:0000255|HAMAP-Rule:MF_00607}; GN OrderedLocusNames=HP_1431; OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=85962; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700392 / 26695; RX PubMed=9252185; DOI=10.1038/41483; RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A., RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.; RT "The complete genome sequence of the gastric pathogen Helicobacter RT pylori."; RL Nature 388:539-547(1997). CC -!- FUNCTION: Specifically dimethylates two adjacent adenosines (A1518 and CC A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA CC in the 30S particle. May play a critical role in biogenesis of 30S CC subunits. {ECO:0000255|HAMAP-Rule:MF_00607}. CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L- CC methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)- CC dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:19609, Rhea:RHEA-COMP:10232, Rhea:RHEA-COMP:10233, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74493; EC=2.1.1.182; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00607}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00607}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. rRNA adenine N(6)-methyltransferase family. RsmA CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00607}. 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; AE000511; AAD08470.1; -; Genomic_DNA. DR PIR; G64698; G64698. DR RefSeq; NP_208222.1; NC_000915.1. DR RefSeq; WP_000259453.1; NC_018939.1. DR AlphaFoldDB; O25972; -. DR SMR; O25972; -. DR STRING; 85962.HP_1431; -. DR PaxDb; 85962-C694_07400; -. DR EnsemblBacteria; AAD08470; AAD08470; HP_1431. DR KEGG; hpy:HP_1431; -. DR PATRIC; fig|85962.47.peg.1535; -. DR eggNOG; COG0030; Bacteria. DR InParanoid; O25972; -. DR OrthoDB; 9814755at2; -. DR PhylomeDB; O25972; -. DR Proteomes; UP000000429; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0052908; F:16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IBA:GO_Central. DR GO; GO:0031167; P:rRNA methylation; IBA:GO_Central. DR CDD; cd02440; AdoMet_MTases; 1. DR Gene3D; 1.10.8.100; Ribosomal RNA adenine dimethylase-like, domain 2; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR HAMAP; MF_00607; 16SrRNA_methyltr_A; 1. DR InterPro; IPR001737; KsgA/Erm. DR InterPro; IPR023165; rRNA_Ade_diMease-like_C. DR InterPro; IPR020596; rRNA_Ade_Mease_Trfase_CS. DR InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N. DR InterPro; IPR011530; rRNA_adenine_dimethylase. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR NCBIfam; TIGR00755; ksgA; 1. DR PANTHER; PTHR11727; DIMETHYLADENOSINE TRANSFERASE; 1. DR PANTHER; PTHR11727:SF7; DIMETHYLADENOSINE TRANSFERASE-RELATED; 1. DR Pfam; PF00398; RrnaAD; 1. DR SMART; SM00650; rADc; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR PROSITE; PS01131; RRNA_A_DIMETH; 1. DR PROSITE; PS51689; SAM_RNA_A_N6_MT; 1. PE 3: Inferred from homology; KW Cytoplasm; Methyltransferase; Reference proteome; RNA-binding; KW rRNA processing; S-adenosyl-L-methionine; Transferase. FT CHAIN 1..271 FT /note="Ribosomal RNA small subunit methyltransferase A" FT /id="PRO_0000101540" FT BINDING 11 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607" FT BINDING 13 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607" FT BINDING 38 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607" FT BINDING 58 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607" FT BINDING 86 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607" FT BINDING 101 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607" SQ SEQUENCE 271 AA; 30644 MW; 870D11C671A7DB91 CRC64; MVVAKKSLGQ HFLTDESFLD RIVNALPPLN PLKLVEIGVG LGDLTLKLLD RYPLKTYEID SHLCEKMRSK LKAQKKPFKL ELVEKDALFL KEEEPYFLIS NLPYYIATRL VLNAFKDPKC RGLLVMTQKE VALKFCAKDS QNALSVLAHT IGNATLLFDV PPSAFSPPPK VFSSVFEVIK EPLKEKALAS LAQAPFFEEA LQKGFEMLED FLKACFSSPR KTLSNNLKKS VSYREKLDKV LDFLALENQP TSVRASEIKD YLKLLNYLLK G //