ID   GRM_MICEC               Reviewed;         274 AA.
AC   P24618;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 61.
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=grmA;
OS   Micromonospora echinospora (Micromonospora purpurea).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Micromonospora.
OX   NCBI_TaxID=1877;
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).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=19589804; DOI=10.1093/nar/gkp575;
RA   Savic M., Lovric J., Tomic T.I., Vasiljevic B., Conn G.L.;
RT   "Determination of the target nucleosides for members of two families of 16S
RT   rRNA methyltransferases that confer resistance to partially overlapping
RT   groups of aminoglycoside antibiotics.";
RL   Nucleic Acids Res. 37:5420-5431(2009).
CC   -!- FUNCTION: Specifically methylates the N(7) position of guanine 1405 in
CC       16S rRNA. Confers resistance to various aminoglycosides, including
CC       gentamicin and kanamycin. {ECO:0000269|PubMed:19589804,
CC       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         Evidence={ECO:0000269|PubMed:19589804};
CC   -!- MISCELLANEOUS: Protects M.echinospora, 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; M55520; AAA25336.1; -; Genomic_DNA.
DR   PIR; JG0017; JG0017.
DR   AlphaFoldDB; P24618; -.
DR   SMR; P24618; -.
DR   KEGG; ag:AAA25336; -.
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_0000083854"
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;  30542 MW;  9D7289559621A68E CRC64;
     MTTSAPEDRI DQVEQAITKS RRYQTVAPAT VRRLARAALV AARGDVPDAV KRTKRGLHEI
     YGAFLPPSPP NYAALLRQLD SAVDAGDDEA VRAALRRAMS VHVSTRERLP HLAEFYQEIF
     RHVPQPNTLR DLACGLNPLA APWMGLSDQT VYVASDIDAR LIGFVDAALT RLGVAHRTSV
     VDLLEDRLDE PTDVTLLLKT LPCLETQRRG SGWEVIDIVN SPIIVVTFPT KSLGQRSKGM
     FQNYSQSFES QARERSCRIQ RLEIGNELIY VIQK