ID RSMA_ACTP2 Reviewed; 289 AA.
AC A3MZB7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 103.
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=APL_0399;
OS Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=416269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L20;
RX PubMed=18065534; DOI=10.1128/jb.01845-07;
RA Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA Nash J.H.E.;
RT "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT (serotype 5b).";
RL J. Bacteriol. 190:1495-1496(2008).
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}.
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DR EMBL; CP000569; ABN73503.1; -; Genomic_DNA.
DR RefSeq; WP_005596422.1; NC_009053.1.
DR AlphaFoldDB; A3MZB7; -.
DR SMR; A3MZB7; -.
DR STRING; 416269.APL_0399; -.
DR EnsemblBacteria; ABN73503; ABN73503; APL_0399.
DR GeneID; 69417576; -.
DR KEGG; apl:APL_0399; -.
DR eggNOG; COG0030; Bacteria.
DR HOGENOM; CLU_041220_0_1_6; -.
DR Proteomes; UP000001432; 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..289
FT /note="Ribosomal RNA small subunit methyltransferase A"
FT /id="PRO_1000056591"
FT BINDING 21
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
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 48
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT BINDING 69
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT BINDING 94
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT BINDING 120
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
SQ SEQUENCE 289 AA; 33272 MW; 5FAD97EC6BBB2B5D CRC64;
MSNQNSKKHL GHTARKRFGQ NFLHDMNVIH NIVSAINPKN GQFLLEIGPG LGALTEPVAE
QVDKLTVVEL DRDLAERLRH HPFLNHKLTI IEQDALRFNF REYFESLELR EGEGVRVFGN
LPYNISTPLM FHLFKFHDLI QDMHFMLQKE VVKRLCAAPN SKAYGRLTIM AQYYCQVMPV
LEVPPTAFKP APKVDSAVVR LMPHKVLPHP VKDVYWLNRV TTQAFNQRRK TLRNALSTLF
SPEQLEALNI DLNARAENLS IADYARLANW LYDNPPAVDN QEEIIDEDI
//
