ID   RLMA2_STRFR             Reviewed;         280 AA.
AC   Q9S1M6; Q9ZHQ6;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=23S rRNA (guanine(748)-N(1))-methyltransferase;
DE            EC=2.1.1.188;
DE   AltName: Full=23S rRNA m1G748 methyltransferase;
DE   AltName: Full=Tylosin-resistance methyltransferase RlmA(II);
GN   Name=rlmAII; Synonyms=tlrB;
OS   Streptomyces fradiae (Streptomyces roseoflavus).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN ANTIBIOTIC RESISTANCE.
RC   STRAIN=C373.1;
RX   PubMed=10348045; DOI=10.7164/antibiotics.52.288;
RA   Wilson V.T., Cundliffe E.;
RT   "Molecular analysis of tlrB, an antibiotic-resistance gene from tylosin-
RT   producing Streptomyces fradiae, and discovery of a novel resistance
RT   mechanism.";
RL   J. Antibiot. 52:288-296(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 19609;
RX   PubMed=10220165; DOI=10.1099/13500872-145-4-855;
RA   Fouces R., Mellado E., Diez B., Barredo J.L.;
RT   "The tylosin biosynthetic cluster from Streptomyces fradiae: genetic
RT   organization of the left region.";
RL   Microbiology 145:855-868(1999).
RN   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 19609;
RX   PubMed=10972803; DOI=10.1046/j.1365-2958.2000.02046.x;
RA   Liu M., Kirpekar F., Van Wezel G.P., Douthwaite S.;
RT   "The tylosin resistance gene tlrB of Streptomyces fradiae encodes a
RT   methyltransferase that targets G748 in 23S rRNA.";
RL   Mol. Microbiol. 37:811-820(2000).
RN   [4]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=15046978; DOI=10.1016/j.jmb.2004.02.030;
RA   Douthwaite S., Crain P.F., Liu M., Poehlsgaard J.;
RT   "The tylosin-resistance methyltransferase RlmA(II) (TlrB) modifies the N-1
RT   position of 23S rRNA nucleotide G748.";
RL   J. Mol. Biol. 337:1073-1077(2004).
CC   -!- FUNCTION: Specifically methylates the guanosine in position 748 of 23S
CC       rRNA. Confers resistance to the macrolide antibiotic tylosine.
CC       {ECO:0000269|PubMed:10348045, ECO:0000269|PubMed:10972803,
CC       ECO:0000269|PubMed:15046978}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(748) in 23S rRNA + S-adenosyl-L-methionine = H(+) +
CC         N(1)-methylguanosine(748) in 23S rRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42904, Rhea:RHEA-COMP:10275, Rhea:RHEA-COMP:10276,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.188;
CC         Evidence={ECO:0000269|PubMed:10972803, ECO:0000269|PubMed:15046978};
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmA family.
CC       {ECO:0000305}.
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DR   EMBL; AJ009971; CAB37345.2; -; Genomic_DNA.
DR   EMBL; AF055922; AAD12162.1; -; Genomic_DNA.
DR   RefSeq; WP_043470786.1; NZ_MCNU01000172.1.
DR   RefSeq; WP_063844496.1; NG_047774.1.
DR   AlphaFoldDB; Q9S1M6; -.
DR   SMR; Q9S1M6; -.
DR   STRING; 1906.SFRA_26480; -.
DR   KEGG; ag:CAB37345; -.
DR   eggNOG; COG2226; Bacteria.
DR   OMA; MTPHGWR; -.
DR   BRENDA; 2.1.1.188; 5932.
DR   GO; GO:0052912; F:23S rRNA (guanine(748)-N(1))-methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070475; P:rRNA base methylation; IDA:UniProtKB.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR041698; Methyltransf_25.
DR   InterPro; IPR016718; rRNA_m1G-MeTrfase_A_prd.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF13649; Methyltransf_25; 1.
DR   PIRSF; PIRSF018249; MyrA_prd; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   1: Evidence at protein level;
KW   Metal-binding; Methyltransferase; rRNA processing; S-adenosyl-L-methionine;
KW   Transferase; Zinc.
FT   CHAIN           1..280
FT                   /note="23S rRNA (guanine(748)-N(1))-methyltransferase"
FT                   /id="PRO_0000419019"
FT   BINDING         11
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         14
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         27
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         31
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         70
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         100..101
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   VARIANT         82
FT                   /note="R -> G (in strain: ATCC 19609)"
SQ   SEQUENCE   280 AA;  30543 MW;  DC7E039037EBFFFD CRC64;
     MRKNVVRYLR CPHCAAPLRS SDRTLRCENG HTFDVARQGY VNLLRRPTKL AADTTDMVAA
     RAALLDSGHY APLTERLAGT ARRAAGAGAP DCVVDIGGGT GHHLARVLEE FEDAEGLLLD
     MSKPAVRRAA RAHPRASSAV ADVWDTLPLR DGAAAMALNV FAPRNPPEIR RILRPGGTLL
     VVTPQQDHLA ELVDALGLLR VRDHKEGRLA EQLAPHFEAV GQERLRTTLR LDHDALGRVV
     AMGPSSWHQD PDELARRIAE LPGIHEVTLS VTFTVCRPLP