GRM_MICRO
ID GRM_MICRO Reviewed; 274 AA.
AC P24619;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=16S rRNA (guanine(1405)-N(7))-methyltransferase;
DE EC=2.1.1.179;
DE AltName: Full=16S rRNA m7G1405 methyltransferase;
DE AltName: Full=Gentamicin-resistance methyltransferase;
GN Name=grm; Synonyms=grmB;
OS Micromonospora rosea.
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Micromonospora.
OX NCBI_TaxID=1878;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN ANTIBIOTIC RESISTANCE.
RX PubMed=2013410; DOI=10.1016/0378-1119(91)90103-i;
RA Kelemen G.H., Cundliffe E., Financsek I.;
RT "Cloning and characterization of gentamicin-resistance genes from
RT Micromonospora purpurea and Micromonospora rosea.";
RL Gene 98:53-60(1991).
CC -!- FUNCTION: Specifically methylates the N(7) position of guanine 1405 in
CC 16S rRNA (By similarity). Confers resistance to aminoglycosides.
CC {ECO:0000250, ECO:0000269|PubMed:2013410}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(1405) in 16S rRNA + S-adenosyl-L-methionine = N(7)-
CC methylguanosine(1405) in 16S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42772, Rhea:RHEA-COMP:10225, Rhea:RHEA-COMP:10226,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:74480; EC=2.1.1.179;
CC -!- MISCELLANEOUS: Protects M.rosea, which is an antibiotic-producing
CC bacterium, against self-intoxication.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC Aminoglycoside resistance family. {ECO:0000305}.
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DR EMBL; M55521; AAA25338.1; -; Genomic_DNA.
DR RefSeq; WP_063851283.1; NG_047907.1.
DR AlphaFoldDB; P24619; -.
DR SMR; P24619; -.
DR BRENDA; 2.1.1.179; 13019.
DR GO; GO:0008649; F:rRNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025981; rRNA_MeTrfase.
DR InterPro; IPR010769; rRNA_MeTrfase_GmN_bac.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF07091; FmrO; 1.
DR PIRSF; PIRSF015852; RRNA_mtase_Grm; 1.
PE 1: Evidence at protein level;
KW Antibiotic resistance; Methyltransferase; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..274
FT /note="16S rRNA (guanine(1405)-N(7))-methyltransferase"
FT /id="PRO_0000083855"
FT BINDING 64
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 102..104
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 182..183
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 274 AA; 30722 MW; D9A7257C2D04D4F9 CRC64;
MTTSTGDDRI DQLQQAITKS RRYQTVAPAT VRRLARAALV ASRGDVPDAV KRTKRGLHEI
YGAFLPPSAP NYTALLRHLD SAVEAGDDEA VVRWDRRAMS VHMSTRERVP HLDEFYREIF
RHVPRPNTLR DLACGLNPLA VPWMGLSDET VYVASDIDAR LMDFVGAALT RLGVAHRTSV
VDLLEARLDE PADVTLLLKT LPCLETQQRG SGWEVIDIVN SPIIVVTFPT KSLGQRSKGM
FQNYSQSFES QASERSCRIQ RLEIGNELIY VIHK
