GENTAUR Molecular Products.

 V5P151_LACJH            Unreviewed;       296 AA.
 V5P151;
 19-FEB-2014, integrated into UniProtKB/TrEMBL.
 19-FEB-2014, sequence version 1.
 28-MAR-2018, entry version 30.
 RecName: Full=Ribosomal RNA small subunit methyltransferase A {ECO:0000256|HAMAP-Rule:MF_00607};
          EC=2.1.1.182 {ECO:0000256|HAMAP-Rule:MF_00607};
 AltName: Full=16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase {ECO:0000256|HAMAP-Rule:MF_00607};
 AltName: Full=16S rRNA dimethyladenosine transferase {ECO:0000256|HAMAP-Rule:MF_00607};
 AltName: Full=16S rRNA dimethylase {ECO:0000256|HAMAP-Rule:MF_00607};
 AltName: Full=S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase {ECO:0000256|HAMAP-Rule:MF_00607};
 Name=rsmA {ECO:0000256|HAMAP-Rule:MF_00607};
 Synonyms=ksgA {ECO:0000256|HAMAP-Rule:MF_00607};
 ORFNames=T285_01145 {ECO:0000313|EMBL:AHA96713.1};
 Lactobacillus johnsonii N6.2.
 Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
 Lactobacillus.
 NCBI_TaxID=1408186 {ECO:0000313|EMBL:AHA96713.1, ECO:0000313|Proteomes:UP000018522};
 [1] {ECO:0000313|EMBL:AHA96713.1, ECO:0000313|Proteomes:UP000018522}
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=N6.2 {ECO:0000313|EMBL:AHA96713.1};
 PubMed=24812223;
 Leonard M.T., Valladares R.B., Ardissone A., Gonzalez C.F.,
 Lorca G.L., Triplett E.W.;
 "Complete Genome Sequences of Lactobacillus johnsonii Strain N6.2 and
 Lactobacillus reuteri Strain TD1.";
 Genome Announc. 2:e00397-14(2014).
 -!- FUNCTION: Specifically dimethylates two adjacent adenosines (A1518
     and A1519) in the loop of a conserved hairpin near the 3'-end of
     16S rRNA in the 30S particle. May play a critical role in
     biogenesis of 30S subunits. {ECO:0000256|HAMAP-Rule:MF_00607}.
 -!- CATALYTIC ACTIVITY: 4 S-adenosyl-L-methionine +
     adenine(1518)/adenine(1519) in 16S rRNA = 4 S-adenosyl-L-
     homocysteine + N(6)-dimethyladenine(1518)/N(6)-
     dimethyladenine(1519) in 16S rRNA. {ECO:0000256|HAMAP-
     Rule:MF_00607}.
 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00607,
     ECO:0000256|SAAS:SAAS00633798}.
 -!- SIMILARITY: Belongs to the class I-like SAM-binding
     methyltransferase superfamily. rRNA adenine N(6)-methyltransferase
     family. RsmA subfamily. {ECO:0000256|HAMAP-Rule:MF_00607,
     ECO:0000256|SAAS:SAAS00633788}.
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 EMBL; CP006811; AHA96713.1; -; Genomic_DNA.
 RefSeq; WP_011161402.1; NC_022909.1.
 ProteinModelPortal; V5P151; -.
 SMR; V5P151; -.
 EnsemblBacteria; AHA96713; AHA96713; T285_01145.
 KEGG; ljn:T285_01145; -.
 PATRIC; fig|1408186.3.peg.220; -.
 KO; K02528; -.
 Proteomes; UP000018522; Chromosome.
 GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO; GO:0052908; F:16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase activity; IEA:UniProtKB-EC.
 GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
 GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IEA:UniProtKB-UniRule.
 Gene3D; 1.10.8.100; -; 1.
 HAMAP; MF_00607; 16SrRNA_methyltr_A; 1.
 InterPro; IPR001737; KsgA/Erm.
 InterPro; IPR023165; rRNA_Ade_diMease-like.
 InterPro; IPR020596; rRNA_Ade_Mease_Trfase_CS.
 InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N.
 InterPro; IPR011530; rRNA_adenine_dimethylase.
 InterPro; IPR029063; SAM-dependent_MTases.
 PANTHER; PTHR11727; PTHR11727; 1.
 Pfam; PF00398; RrnaAD; 1.
 SMART; SM00650; rADc; 1.
 SUPFAM; SSF53335; SSF53335; 1.
 TIGRFAMs; TIGR00755; ksgA; 1.
 PROSITE; PS01131; RRNA_A_DIMETH; 1.
 PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
 3: Inferred from homology;
 Complete proteome {ECO:0000313|Proteomes:UP000018522};
 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00607,
 ECO:0000256|SAAS:SAAS00633772};
 Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00607,
 ECO:0000256|PROSITE-ProRule:PRU01026, ECO:0000256|SAAS:SAAS00633775,
 ECO:0000313|EMBL:AHA96713.1};
 RNA-binding {ECO:0000256|HAMAP-Rule:MF_00607, ECO:0000256|PROSITE-
 ProRule:PRU01026, ECO:0000256|SAAS:SAAS00633771};
 rRNA processing {ECO:0000256|HAMAP-Rule:MF_00607,
 ECO:0000256|SAAS:SAAS00644568};
 S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00607,
 ECO:0000256|PROSITE-ProRule:PRU01026, ECO:0000256|SAAS:SAAS00633825};
 Transferase {ECO:0000256|HAMAP-Rule:MF_00607, ECO:0000256|PROSITE-
 ProRule:PRU01026, ECO:0000256|SAAS:SAAS00633775,
 ECO:0000313|EMBL:AHA96713.1}.
 DOMAIN       38    221       rADc. {ECO:0000259|SMART:SM00650}.
 BINDING      31     31       S-adenosyl-L-methionine; via carbonyl
                              oxygen. {ECO:0000256|HAMAP-Rule:MF_00607,
                              ECO:0000256|PROSITE-ProRule:PRU01026}.
 BINDING      33     33       S-adenosyl-L-methionine; via amide
                              nitrogen. {ECO:0000256|HAMAP-
                              Rule:MF_00607, ECO:0000256|PROSITE-
                              ProRule:PRU01026}.
 BINDING      58     58       S-adenosyl-L-methionine; via carbonyl
                              oxygen. {ECO:0000256|HAMAP-Rule:MF_00607,
                              ECO:0000256|PROSITE-ProRule:PRU01026}.
 BINDING      79     79       S-adenosyl-L-methionine.
                              {ECO:0000256|HAMAP-Rule:MF_00607,
                              ECO:0000256|PROSITE-ProRule:PRU01026}.
 BINDING     111    111       S-adenosyl-L-methionine.
                              {ECO:0000256|HAMAP-Rule:MF_00607,
                              ECO:0000256|PROSITE-ProRule:PRU01026}.
 BINDING     136    136       S-adenosyl-L-methionine.
                              {ECO:0000256|HAMAP-Rule:MF_00607,
                              ECO:0000256|PROSITE-ProRule:PRU01026}.
 SEQUENCE   296 AA;  33331 MW;  11F6C96919E08F9A CRC64;
 MSNSMPIASP VRTQAIVNRY FMHAKKNLGQ NFLVDLPAIK GIVEAADIQP GDQVIEIGPG
 IGSLTEQLLL AGAKVLAYEV DQDLPEILNN ELPQKIDGEE LKDRFKLVMK DVLKANFVED
 NDGFLDLSKS VKIVANLPYY ITTPIIFNLI KSDLDFSSLT LMMQKEVAER LVAKPKTKEY
 GPLSIAVQSR MNVRLAEEVK STSFMPRPKV DSAVVVLTPL LEKPDINDYA FFDHVVKMCF
 AQRRKTLANN LKTLIKDKDE REKLINDLGL DVRVRPEELT LNQFVQLAHL LKDRQA

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