ID RSMA_RICPR Reviewed; 268 AA. AC O05952; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 27-MAR-2024, entry version 125. 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=RP672; OS Rickettsia prowazekii (strain Madrid E). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group. OX NCBI_TaxID=272947; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Madrid E; RX PubMed=9274032; DOI=10.1099/00221287-143-8-2783; RA Andersson J.O., Andersson S.G.E.; RT "Genomic rearrangements during evolution of the obligate intracellular RT parasite Rickettsia prowazekii as inferred from an analysis of 52015 bp RT nucleotide sequence."; RL Microbiology 143:2783-2795(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Madrid E; RX PubMed=9823893; DOI=10.1038/24094; RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., RA Kurland C.G.; RT "The genome sequence of Rickettsia prowazekii and the origin of RT mitochondria."; RL Nature 396:133-140(1998). 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; Y11786; CAA72482.1; -; Genomic_DNA. DR EMBL; AJ235272; CAA15109.1; -; Genomic_DNA. DR PIR; C71673; C71673. DR RefSeq; NP_221033.1; NC_000963.1. DR RefSeq; WP_004599528.1; NC_000963.1. DR AlphaFoldDB; O05952; -. DR SMR; O05952; -. DR STRING; 272947.gene:17555749; -. DR EnsemblBacteria; CAA15109; CAA15109; CAA15109. DR GeneID; 57569798; -. DR KEGG; rpr:RP672; -. DR PATRIC; fig|272947.5.peg.693; -. DR eggNOG; COG0030; Bacteria. DR HOGENOM; CLU_041220_0_1_5; -. DR OrthoDB; 9814755at2; -. DR Proteomes; UP000002480; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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 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..268 FT /note="Ribosomal RNA small subunit methyltransferase A" FT /id="PRO_0000101595" FT BINDING 23 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607" FT BINDING 25 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607" FT BINDING 50 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607" FT BINDING 72 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607" FT BINDING 97 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607" FT BINDING 116 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607" SQ SEQUENCE 268 AA; 30306 MW; AF2D364DA5093192 CRC64; MLPSIVKHAT SHKINPLKKH GQNFIFDSSL CDKIIRASNV LENSNVIEIG PGIGGLTRSI LQKNPKSLTV IEIDERCIPL LNEIQEYYPN LNIIKQDVLK INLTDLIYDK VTVISNLPYH IGTELVIRLL KEVKLITNMT LMLQKEVVER ICAIPSTKAY GRLSVICQIL AKVEKCFNVA PTAFYPHPKV YSAIVKIIPL ENPPSIALIN KVEQITKLVF AGRRKMIKSS LRNLIPNIHE VLTQLKINCN DRAENLTPKD YLRIAMKL //