RMTC_PROMI
ID RMTC_PROMI Reviewed; 281 AA.
AC Q33DX5;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 55.
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=rmtC;
OS Proteus mirabilis.
OG Plasmid pARS68.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=584;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-5, FUNCTION IN
RP ANTIBIOTIC RESISTANCE AND AS A METHYLTRANSFERASE, AND GENE NAME.
RC STRAIN=ARS68; PLASMID=pARS68;
RX PubMed=16377684; DOI=10.1128/aac.50.1.178-184.2006;
RA Wachino J., Yamane K., Shibayama K., Kurokawa H., Shibata N., Suzuki S.,
RA Doi Y., Kimura K., Ike Y., Arakawa Y.;
RT "Novel plasmid-mediated 16S rRNA methylase, RmtC, found in a proteus
RT mirabilis isolate demonstrating extraordinary high-level resistance against
RT various aminoglycosides.";
RL Antimicrob. Agents Chemother. 50:178-184(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JIE273;
RX PubMed=18025117; DOI=10.1128/aac.01399-07;
RA Zong Z., Partridge S.R., Iredell J.R.;
RT "RmtC 16S rRNA methyltransferase in Australia.";
RL Antimicrob. Agents Chemother. 52:794-795(2008).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ARS68; PLASMID=pARS68;
RX PubMed=20722735; DOI=10.1111/j.1574-6968.2010.02068.x;
RA Wachino J., Shibayama K., Kimura K., Yamane K., Suzuki S., Arakawa Y.;
RT "RmtC introduces G1405 methylation in 16S rRNA and confers high-level
RT aminoglycoside resistance on Gram-positive microorganisms.";
RL FEMS Microbiol. Lett. 311:56-60(2010).
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:16377684,
CC ECO:0000269|PubMed:20722735}.
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:20722735};
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC Aminoglycoside resistance family. {ECO:0000305}.
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DR EMBL; AB194779; BAE48305.1; -; Genomic_DNA.
DR EMBL; EU144360; ABX39521.1; -; Genomic_DNA.
DR RefSeq; WP_000855769.1; NG_048060.1.
DR PDB; 6CN0; X-ray; 2.95 A; A/B/C/D=1-281.
DR PDB; 6PQB; X-ray; 3.14 A; A/B/C/D=1-281.
DR PDBsum; 6CN0; -.
DR PDBsum; 6PQB; -.
DR AlphaFoldDB; Q33DX5; -.
DR SMR; Q33DX5; -.
DR KEGG; ag:BAE48305; -.
DR BRENDA; 2.1.1.179; 5044.
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 3D-structure; Antibiotic resistance; Direct protein sequencing;
KW Methyltransferase; Plasmid; rRNA processing; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..281
FT /note="16S rRNA (guanine(1405)-N(7))-methyltransferase"
FT /id="PRO_0000416819"
FT BINDING 60
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 105..107
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 136
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 186..187
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT HELIX 4..17
FT /evidence="ECO:0007829|PDB:6CN0"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:6PQB"
FT HELIX 26..36
FT /evidence="ECO:0007829|PDB:6CN0"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:6CN0"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:6CN0"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:6CN0"
FT HELIX 66..79
FT /evidence="ECO:0007829|PDB:6CN0"
FT HELIX 87..102
FT /evidence="ECO:0007829|PDB:6CN0"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:6CN0"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:6CN0"
FT HELIX 115..126
FT /evidence="ECO:0007829|PDB:6CN0"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:6CN0"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:6CN0"
FT HELIX 144..149
FT /evidence="ECO:0007829|PDB:6CN0"
FT STRAND 154..161
FT /evidence="ECO:0007829|PDB:6CN0"
FT HELIX 163..175
FT /evidence="ECO:0007829|PDB:6CN0"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:6CN0"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:6CN0"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:6CN0"
FT HELIX 206..212
FT /evidence="ECO:0007829|PDB:6CN0"
FT HELIX 216..223
FT /evidence="ECO:0007829|PDB:6CN0"
FT STRAND 227..234
FT /evidence="ECO:0007829|PDB:6CN0"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:6CN0"
FT HELIX 249..259
FT /evidence="ECO:0007829|PDB:6CN0"
FT STRAND 263..270
FT /evidence="ECO:0007829|PDB:6CN0"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:6CN0"
SQ SEQUENCE 281 AA; 32106 MW; BA1342B4A198A7AE CRC64;
MKTNDNYIEE VTAKVLTSGK YSTLYPPTVR RVTERLFDRY PPKQLEKEVR KKLHQAYGAY
IGGIDGKRLE KKIEKIIHEI PNPTTDEATR TEWEKEICLK ILNLHTSTNE RTVAYDELYQ
KIFEVTGVPT SITDAGCALN PFSFPFFTEA GMLGQYIGFD LDKGMIEAIE HSLRTLNAPE
GIVVKQGDIL SDPSGESDLL LMFKLYTLLD RQEEASGLKI LQEWKYKNAV ISFPIKTISG
RDVGMEENYT VKFENDLVGS DLRIMQKLKL GNEMYFIVSR L
