ID   FMRO_MICOL              Reviewed;         293 AA.
AC   Q08325;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 2.
DT   03-AUG-2022, entry version 58.
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=Fortimicin A-resistance methyltransferase;
GN   Name=fmrO;
OS   Micromonospora olivasterospora.
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Micromonospora.
OX   NCBI_TaxID=1880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN ANTIBIOTIC RESISTANCE.
RX   PubMed=8486289; DOI=10.1016/0378-1119(93)90617-c;
RA   Ohta T., Hasegawa M.;
RT   "Analysis of the self-defense gene (fmrO) of a fortimicin A (astromicin)
RT   producer, Micromonospora olivasterospora: comparison with other
RT   aminoglycoside-resistance-encoding genes.";
RL   Gene 127:63-69(1993).
RN   [2]
RP   SEQUENCE REVISION TO 189-208.
RA   Ohta T., Hasegawa M.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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:8486289}.
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.olivasterospora, which is an antibiotic-
CC       producing bacterium, against self-intoxication.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       Aminoglycoside resistance family. {ECO:0000305}.
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DR   EMBL; D13171; BAA02451.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q08325; -.
DR   SMR; Q08325; -.
DR   BRENDA; 2.1.1.179; 12910.
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.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   1: Evidence at protein level;
KW   Antibiotic resistance; Methyltransferase; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..293
FT                   /note="16S rRNA (guanine(1405)-N(7))-methyltransferase"
FT                   /id="PRO_0000087316"
FT   REGION          258..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         47
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         80..82
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         86
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         111
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         134
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         160..161
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         176
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         185
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   293 AA;  30922 MW;  19D5E65F3B9E43D5 CRC64;
     MLAAAKYRNL DPAFVERLAQ EAAERFRDRG QAVKYAKRKL HQAFGAFVAG TPAQAVAACV
     AKIAAGAEPK EAGREAMRAH ASSAERVDWL EPFYERVAQW CGPASSVIDL ACGLNPLAVP
     WMALAPGATY ACYDVDRTMA EALRALGTVY PVRVNAAAVD LVAAVPAAGV DVALVLKTLT
     TVEQQRGGRR VAEYRRELTA VQHHSDGARS LSGRRGYADD PDAIVQRAVH GTGYEVVDEA
     AFGTEALYHL VPLAGTAGRP APAEGAAEPG ATRPVVDVPA TARPDADRVD PTG