RSMA_BURPS
ID RSMA_BURPS Reviewed; 275 AA.
AC Q63X76;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=BPSL0661;
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
RG Seattle structural genomics center for infectious disease (SSGCID);
RT "The structure of the ribosomal RNA small subunit methyltransferase A from
RT Burkholderia pseudomallei.";
RL Submitted (DEC-2011) to the PDB data bank.
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; BX571965; CAH34654.1; -; Genomic_DNA.
DR RefSeq; WP_004189099.1; NZ_CP009538.1.
DR RefSeq; YP_107290.1; NC_006350.1.
DR PDB; 3UZU; X-ray; 1.75 A; A=1-275.
DR PDBsum; 3UZU; -.
DR AlphaFoldDB; Q63X76; -.
DR SMR; Q63X76; -.
DR STRING; 272560.BPSL0661; -.
DR EnsemblBacteria; CAH34654; CAH34654; BPSL0661.
DR GeneID; 56596644; -.
DR KEGG; bps:BPSL0661; -.
DR PATRIC; fig|272560.51.peg.959; -.
DR eggNOG; COG0030; Bacteria.
DR OMA; KEEEPYF; -.
DR Proteomes; UP000000605; Chromosome 1.
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; 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; PS51689; SAM_RNA_A_N6_MT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW RNA-binding; rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..275
FT /note="Ribosomal RNA small subunit methyltransferase A"
FT /id="PRO_0000101503"
FT BINDING 19
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
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 46
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT BINDING 71
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 117
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT HELIX 24..34
FT /evidence="ECO:0007829|PDB:3UZU"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:3UZU"
FT HELIX 53..60
FT /evidence="ECO:0007829|PDB:3UZU"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:3UZU"
FT HELIX 74..84
FT /evidence="ECO:0007829|PDB:3UZU"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:3UZU"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:3UZU"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:3UZU"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:3UZU"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:3UZU"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:3UZU"
FT HELIX 120..130
FT /evidence="ECO:0007829|PDB:3UZU"
FT HELIX 131..136
FT /evidence="ECO:0007829|PDB:3UZU"
FT STRAND 137..145
FT /evidence="ECO:0007829|PDB:3UZU"
FT HELIX 146..152
FT /evidence="ECO:0007829|PDB:3UZU"
FT HELIX 163..171
FT /evidence="ECO:0007829|PDB:3UZU"
FT STRAND 172..180
FT /evidence="ECO:0007829|PDB:3UZU"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:3UZU"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:3UZU"
FT STRAND 193..200
FT /evidence="ECO:0007829|PDB:3UZU"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:3UZU"
FT HELIX 211..221
FT /evidence="ECO:0007829|PDB:3UZU"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:3UZU"
FT HELIX 229..232
FT /evidence="ECO:0007829|PDB:3UZU"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:3UZU"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:3UZU"
FT TURN 242..246
FT /evidence="ECO:0007829|PDB:3UZU"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:3UZU"
FT HELIX 258..271
FT /evidence="ECO:0007829|PDB:3UZU"
SQ SEQUENCE 275 AA; 30247 MW; BAA24F32D1C0985F CRC64;
MSNSRQHQGH FARKRFGQNF LVDHGVIDAI VAAIRPERGE RMVEIGPGLG ALTGPVIARL
ATPGSPLHAV ELDRDLIGRL EQRFGELLEL HAGDALTFDF GSIARPGDEP SLRIIGNLPY
NISSPLLFHL MSFAPVVIDQ HFMLQNEVVE RMVAEPGTKA FSRLSVMLQY RYVMDKLIDV
PPESFQPPPK VDSAIVRMIP HAPHELPAVD PAVLGEVVTA AFSQRRKMLR NTLGGYRDLV
DFDALGFDLA RRAEDIGVDE YVRVAQAVAS ARASG
