ID   KRM_FRACC               Reviewed;         284 AA.
AC   Q2J7L5;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=16S rRNA (guanine(1405)-N(7))-methyltransferase;
DE            EC=2.1.1.179;
DE   AltName: Full=16S rRNA m7G1405 methyltransferase;
GN   Name=Krm; OrderedLocusNames=Francci3_3372;
OS   Frankia casuarinae (strain DSM 45818 / CECT 9043 / CcI3).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=106370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45818 / CECT 9043 / CcI3;
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA   Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA   Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA   Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA   Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA   Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA   Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
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   -!- 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 Frankia sp., 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; CP000249; ABD12727.1; -; Genomic_DNA.
DR   RefSeq; WP_011437753.1; NZ_LRTJ01000095.1.
DR   AlphaFoldDB; Q2J7L5; -.
DR   SMR; Q2J7L5; -.
DR   STRING; 106370.Francci3_3372; -.
DR   EnsemblBacteria; ABD12727; ABD12727; Francci3_3372.
DR   KEGG; fra:Francci3_3372; -.
DR   eggNOG; ENOG5033S4K; Bacteria.
DR   HOGENOM; CLU_1044669_0_0_11; -.
DR   OrthoDB; 1722502at2; -.
DR   BRENDA; 2.1.1.179; 2325.
DR   Proteomes; UP000001937; Chromosome.
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; Reference proteome;
KW   rRNA processing; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..284
FT                   /note="16S rRNA (guanine(1405)-N(7))-methyltransferase"
FT                   /id="PRO_0000416816"
FT   BINDING         73
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         111..113
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         165
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         191..192
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         208
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         217
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   284 AA;  30774 MW;  1F6D34FD23CB5901 CRC64;
     MAVRDGGGSA PVGSQEQAVD RVRETVARSR RYGAVAPETV RRLAERALVA SRGDEPEAVK
     RTKRSLHEIY GAYLPERAPG YPGLLRDIGA AVGGGDPDAV AAAVSRAMRV HASTRERLPY
     LREFYAAVFG AVPTPAVVQD LACGLNPLAF GSMGLPAQTT YLASDIDSQQ MEFLDRALDL
     LEVEHRVEVV DLVSGAVPAQ HADVTLVLKT LPLLERQRAG AGWELVDALR SPFVVVSFPT
     RSLGQRSKGM FQTYSAAFEA QAAERGWTFD QAEIANELIY IVRR