SGM_MICZI
ID SGM_MICZI Reviewed; 274 AA.
AC Q7M0R2;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 49.
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=Sisomicin-gentamicin resistance methylase Sgm;
GN Name=sgm;
OS Micromonospora zionensis.
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Micromonospora.
OX NCBI_TaxID=1879;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN ANTIBIOTIC RESISTANCE.
RX PubMed=1447159; DOI=10.1128/jb.174.23.7868-7872.1992;
RA Kojic M., Topisirovic L., Vasiljevic B.;
RT "Cloning and characterization of an aminoglycoside resistance determinant
RT from Micromonospora zionensis.";
RL J. Bacteriol. 174:7868-7872(1992).
RN [2]
RP INDUCTION.
RX PubMed=8808941; DOI=10.1128/jb.178.18.5493-5498.1996;
RA Kojic M., Topisirovic L., Vasiljevic B.;
RT "Translational autoregulation of the sgm gene from Micromonospora
RT zionensis.";
RL J. Bacteriol. 178:5493-5498(1996).
RN [3]
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE AND S-ADENOSYL-L-HOMOCYSTEINE, AND MUTAGENESIS OF
RP ARG-108; ASP-156 AND ASP-182.
RX PubMed=20194115; DOI=10.1093/nar/gkq122;
RA Husain N., Tkaczuk K.L., Tulsidas S.R., Kaminska K.H., Cubrilo S.,
RA Maravic-Vlahovicek G., Bujnicki J.M., Sivaraman J.;
RT "Structural basis for the methylation of G1405 in 16S rRNA by
RT aminoglycoside resistance methyltransferase Sgm from an antibiotic
RT producer: a diversity of active sites in m7G methyltransferases.";
RL Nucleic Acids Res. 38:4120-4132(2010).
CC -!- FUNCTION: Specifically methylates the N(7) position of guanine 1405 in
CC 16S rRNA. Confers resistance to various aminoglycosides, including
CC gentamicin, kanamycin and sisomicin. {ECO:0000269|PubMed:1447159,
CC 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 -!- INDUCTION: Regulates its expression by binding to its own mRNA.
CC {ECO:0000269|PubMed:8808941}.
CC -!- MISCELLANEOUS: Protects M.zionensis, 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 PIR; A45282; A45282.
DR RefSeq; WP_063978071.1; NG_050600.1.
DR PDB; 3LCU; X-ray; 2.10 A; A=1-274.
DR PDB; 3LCV; X-ray; 2.00 A; B=1-274.
DR PDBsum; 3LCU; -.
DR PDBsum; 3LCV; -.
DR AlphaFoldDB; Q7M0R2; -.
DR SMR; Q7M0R2; -.
DR BRENDA; 2.1.1.179; 11470.
DR EvolutionaryTrace; Q7M0R2; -.
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 3D-structure; 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_0000416817"
FT BINDING 102..108
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:20194115,
FT ECO:0007744|PDB:3LCU"
FT BINDING 133
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:20194115,
FT ECO:0007744|PDB:3LCU"
FT BINDING 156
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:20194115,
FT ECO:0007744|PDB:3LCU"
FT BINDING 182..183
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:20194115,
FT ECO:0007744|PDB:3LCU"
FT BINDING 198
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:20194115,
FT ECO:0007744|PDB:3LCU"
FT BINDING 207
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:20194115,
FT ECO:0007744|PDB:3LCU"
FT MUTAGEN 108
FT /note="R->A: Loss of S-adenosyl-L-methionine binding."
FT /evidence="ECO:0000269|PubMed:20194115"
FT MUTAGEN 156
FT /note="D->A: Loss of S-adenosyl-L-methionine binding."
FT /evidence="ECO:0000269|PubMed:20194115"
FT MUTAGEN 182
FT /note="D->A: Loss of S-adenosyl-L-methionine binding."
FT /evidence="ECO:0000269|PubMed:20194115"
FT HELIX 9..17
FT /evidence="ECO:0007829|PDB:3LCV"
FT TURN 20..25
FT /evidence="ECO:0007829|PDB:3LCV"
FT HELIX 28..41
FT /evidence="ECO:0007829|PDB:3LCV"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:3LCV"
FT HELIX 46..60
FT /evidence="ECO:0007829|PDB:3LCV"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:3LCV"
FT HELIX 72..83
FT /evidence="ECO:0007829|PDB:3LCV"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:3LCV"
FT HELIX 88..99
FT /evidence="ECO:0007829|PDB:3LCV"
FT HELIX 103..108
FT /evidence="ECO:0007829|PDB:3LCV"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:3LCV"
FT HELIX 112..119
FT /evidence="ECO:0007829|PDB:3LCV"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:3LCV"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:3LCV"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:3LCV"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:3LCV"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:3LCV"
FT HELIX 159..171
FT /evidence="ECO:0007829|PDB:3LCV"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:3LCV"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:3LCV"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:3LCV"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:3LCV"
FT HELIX 211..218
FT /evidence="ECO:0007829|PDB:3LCV"
FT STRAND 222..229
FT /evidence="ECO:0007829|PDB:3LCV"
FT HELIX 240..255
FT /evidence="ECO:0007829|PDB:3LCV"
FT STRAND 258..264
FT /evidence="ECO:0007829|PDB:3LCV"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:3LCV"
SQ SEQUENCE 274 AA; 30669 MW; 30D91AFD0A7AE3E7 CRC64;
MTAPAADDRI DEIERAITKS RRYQTVAPAT VRRLARAALV AARGDVPDAV KRTKRGLHEI
YGAFLPPSPP NYAALLRHLD SAVDAGDDEA VRAALLRAMS VHISTRERLP HLDEFYRELF
RHLPRPNTLR DLACGLNPLA APWMGLPAET VYIASDIDAR LVGFVDEALT RLNVPHRTNV
ADLLEDRLDE PADVTLLLKT LPCLETQQRG SGWEVIDIVN SPNIVVTFPT KSLGQRSKGM
FQNYSQSFES QARERSCRIQ RLEIGNELIY VIQK
