RSMA_COXBU
ID RSMA_COXBU Reviewed; 258 AA.
AC Q83AC2;
DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 108.
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=CBU_1982;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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; AE016828; AAO91471.2; -; Genomic_DNA.
DR RefSeq; NP_820957.2; NC_002971.3.
DR RefSeq; WP_005772431.1; NZ_CCYB01000065.1.
DR PDB; 3TQS; X-ray; 1.98 A; A/B/C/D=4-258.
DR PDBsum; 3TQS; -.
DR AlphaFoldDB; Q83AC2; -.
DR SMR; Q83AC2; -.
DR STRING; 227377.CBU_1982; -.
DR EnsemblBacteria; AAO91471; AAO91471; CBU_1982.
DR GeneID; 1209895; -.
DR KEGG; cbu:CBU_1982; -.
DR PATRIC; fig|227377.7.peg.1969; -.
DR eggNOG; COG0030; Bacteria.
DR HOGENOM; CLU_041220_0_1_6; -.
DR OMA; KEEEPYF; -.
DR Proteomes; UP000002671; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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 GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IBA:GO_Central.
DR GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
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 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..258
FT /note="Ribosomal RNA small subunit methyltransferase A"
FT /id="PRO_0000101520"
FT BINDING 13
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT BINDING 15
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT BINDING 40
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT BINDING 61
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT BINDING 86
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT BINDING 106
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT HELIX 18..28
FT /evidence="ECO:0007829|PDB:3TQS"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:3TQS"
FT TURN 42..46
FT /evidence="ECO:0007829|PDB:3TQS"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:3TQS"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:3TQS"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:3TQS"
FT HELIX 64..74
FT /evidence="ECO:0007829|PDB:3TQS"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:3TQS"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:3TQS"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:3TQS"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:3TQS"
FT HELIX 109..121
FT /evidence="ECO:0007829|PDB:3TQS"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:3TQS"
FT STRAND 126..134
FT /evidence="ECO:0007829|PDB:3TQS"
FT HELIX 135..141
FT /evidence="ECO:0007829|PDB:3TQS"
FT HELIX 152..160
FT /evidence="ECO:0007829|PDB:3TQS"
FT STRAND 161..169
FT /evidence="ECO:0007829|PDB:3TQS"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:3TQS"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:3TQS"
FT STRAND 182..189
FT /evidence="ECO:0007829|PDB:3TQS"
FT HELIX 200..212
FT /evidence="ECO:0007829|PDB:3TQS"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:3TQS"
FT TURN 222..225
FT /evidence="ECO:0007829|PDB:3TQS"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:3TQS"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:3TQS"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:3TQS"
FT HELIX 247..257
FT /evidence="ECO:0007829|PDB:3TQS"
SQ SEQUENCE 258 AA; 29779 MW; 40C0F96B085DFD2A CRC64;
MKKMPMRKRF GQHFLHDSFV LQKIVSAIHP QKTDTLVEIG PGRGALTDYL LTECDNLALV
EIDRDLVAFL QKKYNQQKNI TIYQNDALQF DFSSVKTDKP LRVVGNLPYN ISTPLLFHLF
SQIHCIEDMH FMLQKEVVRR ITAEVGSHDY GRLSVMAQYF CDNTYLFTVS PQAFTPPPRV
ESAIIRLIPR HNFTPVAKNL DQLSHVVKEA FSYRRKTVGN ALKKLINPSQ WPLLEINPQL
RPQELTVEDF VKISNILN
