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RSMA_STAEQ
ID   RSMA_STAEQ              Reviewed;         296 AA.
AC   Q5HRR2;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=SERP0131;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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; CP000029; AAW53476.1; -; Genomic_DNA.
DR   RefSeq; WP_001832224.1; NC_002976.3.
DR   AlphaFoldDB; Q5HRR2; -.
DR   SMR; Q5HRR2; -.
DR   STRING; 176279.SERP0131; -.
DR   EnsemblBacteria; AAW53476; AAW53476; SERP0131.
DR   GeneID; 50019596; -.
DR   KEGG; ser:SERP0131; -.
DR   eggNOG; COG0030; Bacteria.
DR   HOGENOM; CLU_041220_0_0_9; -.
DR   OMA; KEEEPYF; -.
DR   OrthoDB; 2030110at2; -.
DR   Proteomes; UP000000531; 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   Gene3D; 1.10.8.100; -; 1.
DR   Gene3D; 3.40.50.150; -; 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   PANTHER; PTHR11727; PTHR11727; 1.
DR   Pfam; PF00398; RrnaAD; 1.
DR   SMART; SM00650; rADc; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00755; ksgA; 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..296
FT                   /note="Ribosomal RNA small subunit methyltransferase A"
FT                   /id="PRO_0000101610"
FT   BINDING         30
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT   BINDING         32
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT   BINDING         57
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT   BINDING         78
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT   BINDING         103
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT   BINDING         128
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
SQ   SEQUENCE   296 AA;  33494 MW;  9FFB2E23ACB7E361 CRC64;
     MEYKDIATPS RTRALLDQYG FNFKKSLGQN FLIDVNIINK IIEASHIDCT TGVIEVGPGM
     GSLTEQLAKN AKKVMAFEID QRLIPVLKDT LSPYDNVTII NEDILKADIA KAVDTHLQDC
     DKIMVVANLP YYITTPILLN LMQQDVPIDG FVVMMQKEVG ERLNAQVGTK AYGSLSIVAQ
     YYTETSKVLT VPKTVFMPPP NVDSIVVKLM QRQEPLVQVD DEEGFFKLAK AAFAQRRKTI
     NNNYQNFFKD GKKNKETIRQ WLESAGIDPK RRGETLTIQD FATLYEQKKK FSELTN
 
 
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