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16S rRNA (guanine(1405)-N(7))-methyltransferase (EC 2.1.1.179) (16S rRNA m7G1405 methyltransferase) (Sisomicin-gentamicin resistance methylase Sgm)

 SGM_MICZI               Reviewed;         274 AA.
Q7M0R2;
18-APR-2012, integrated into UniProtKB/Swiss-Prot.
15-DEC-2003, sequence version 1.
05-DEC-2018, entry version 43.
RecName: Full=16S rRNA (guanine(1405)-N(7))-methyltransferase;
EC=2.1.1.179;
AltName: Full=16S rRNA m7G1405 methyltransferase;
AltName: Full=Sisomicin-gentamicin resistance methylase Sgm;
Name=sgm;
Micromonospora zionensis.
Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
Micromonospora.
NCBI_TaxID=1879;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN ANTIBIOTIC
RESISTANCE.
PubMed=1447159; DOI=10.1128/jb.174.23.7868-7872.1992;
Kojic M., Topisirovic L., Vasiljevic B.;
"Cloning and characterization of an aminoglycoside resistance
determinant from Micromonospora zionensis.";
J. Bacteriol. 174:7868-7872(1992).
[2]
INDUCTION.
PubMed=8808941; DOI=10.1128/jb.178.18.5493-5498.1996;
Kojic M., Topisirovic L., Vasiljevic B.;
"Translational autoregulation of the sgm gene from Micromonospora
zionensis.";
J. Bacteriol. 178:5493-5498(1996).
[3]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=19589804; DOI=10.1093/nar/gkp575;
Savic M., Lovric J., Tomic T.I., Vasiljevic B., Conn G.L.;
"Determination of the target nucleosides for members of two families
of 16S rRNA methyltransferases that confer resistance to partially
overlapping groups of aminoglycoside antibiotics.";
Nucleic Acids Res. 37:5420-5431(2009).
[4]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH
S-ADENOSYL-L-METHIONINE AND S-ADENOSYL-L-HOMOCYSTEINE, AND MUTAGENESIS
OF ARG-108; ASP-156 AND ASP-182.
PubMed=20194115; DOI=10.1093/nar/gkq122;
Husain N., Tkaczuk K.L., Tulsidas S.R., Kaminska K.H., Cubrilo S.,
Maravic-Vlahovicek G., Bujnicki J.M., Sivaraman J.;
"Structural basis for the methylation of G1405 in 16S rRNA by
aminoglycoside resistance methyltransferase Sgm from an antibiotic
producer: a diversity of active sites in m7G methyltransferases.";
Nucleic Acids Res. 38:4120-4132(2010).
-!- FUNCTION: Specifically methylates the N(7) position of guanine
1405 in 16S rRNA. Confers resistance to various aminoglycosides,
including gentamicin, kanamycin and sisomicin.
{ECO:0000269|PubMed:1447159, ECO:0000269|PubMed:19589804}.
-!- CATALYTIC ACTIVITY:
Reaction=guanosine(1405) in 16S rRNA + S-adenosyl-L-methionine =
N(7)-methylguanosine(1405) in 16S rRNA + S-adenosyl-L-
homocysteine; Xref=Rhea:RHEA:42772, Rhea:RHEA-COMP:10225,
Rhea:RHEA-COMP:10226, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
ChEBI:CHEBI:74269, ChEBI:CHEBI:74480; EC=2.1.1.179;
Evidence={ECO:0000269|PubMed:19589804};
-!- INDUCTION: Regulates its expression by binding to its own mRNA.
{ECO:0000269|PubMed:8808941}.
-!- MISCELLANEOUS: Protects M.zionensis, which is an antibiotic-
producing bacterium, against self-intoxication.
-!- SIMILARITY: Belongs to the methyltransferase superfamily.
Aminoglycoside resistance family. {ECO:0000305}.
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PIR; A45282; A45282.
RefSeq; WP_063978071.1; NG_050600.1.
PDB; 3LCU; X-ray; 2.10 A; A=1-274.
PDB; 3LCV; X-ray; 2.00 A; B=1-274.
PDBsum; 3LCU; -.
PDBsum; 3LCV; -.
ProteinModelPortal; Q7M0R2; -.
SMR; Q7M0R2; -.
BRENDA; 2.1.1.179; 11470.
EvolutionaryTrace; Q7M0R2; -.
GO; GO:0008649; F:rRNA methyltransferase activity; IEA:InterPro.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
InterPro; IPR025981; rRNA_MeTrfase.
InterPro; IPR010769; rRNA_MeTrfase_GmN_bac.
Pfam; PF07091; FmrO; 1.
PIRSF; PIRSF015852; RRNA_mtase_Grm; 1.
1: Evidence at protein level;
3D-structure; Antibiotic resistance; Methyltransferase;
rRNA processing; S-adenosyl-L-methionine; Transferase.
CHAIN 1 274 16S rRNA (guanine(1405)-N(7))-
methyltransferase.
/FTId=PRO_0000416817.
REGION 102 108 S-adenosyl-L-methionine binding.
{ECO:0000244|PDB:3LCU,
ECO:0000269|PubMed:20194115}.
REGION 182 183 S-adenosyl-L-methionine binding.
{ECO:0000244|PDB:3LCU,
ECO:0000269|PubMed:20194115}.
BINDING 133 133 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000244|PDB:3LCU,
ECO:0000269|PubMed:20194115}.
BINDING 156 156 S-adenosyl-L-methionine.
{ECO:0000244|PDB:3LCU,
ECO:0000269|PubMed:20194115}.
BINDING 198 198 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000244|PDB:3LCU,
ECO:0000269|PubMed:20194115}.
BINDING 207 207 S-adenosyl-L-methionine.
{ECO:0000244|PDB:3LCU,
ECO:0000269|PubMed:20194115}.
MUTAGEN 108 108 R->A: Loss of S-adenosyl-L-methionine
binding. {ECO:0000269|PubMed:20194115}.
MUTAGEN 156 156 D->A: Loss of S-adenosyl-L-methionine
binding. {ECO:0000269|PubMed:20194115}.
MUTAGEN 182 182 D->A: Loss of S-adenosyl-L-methionine
binding. {ECO:0000269|PubMed:20194115}.
HELIX 9 17 {ECO:0000244|PDB:3LCV}.
TURN 20 25 {ECO:0000244|PDB:3LCV}.
HELIX 28 41 {ECO:0000244|PDB:3LCV}.
TURN 42 44 {ECO:0000244|PDB:3LCV}.
HELIX 46 60 {ECO:0000244|PDB:3LCV}.
HELIX 62 64 {ECO:0000244|PDB:3LCV}.
HELIX 72 83 {ECO:0000244|PDB:3LCV}.
TURN 84 86 {ECO:0000244|PDB:3LCV}.
HELIX 88 99 {ECO:0000244|PDB:3LCV}.
HELIX 103 108 {ECO:0000244|PDB:3LCV}.
HELIX 109 111 {ECO:0000244|PDB:3LCV}.
HELIX 112 119 {ECO:0000244|PDB:3LCV}.
HELIX 120 122 {ECO:0000244|PDB:3LCV}.
STRAND 127 131 {ECO:0000244|PDB:3LCV}.
HELIX 137 139 {ECO:0000244|PDB:3LCV}.
TURN 142 144 {ECO:0000244|PDB:3LCV}.
STRAND 151 158 {ECO:0000244|PDB:3LCV}.
HELIX 159 171 {ECO:0000244|PDB:3LCV}.
STRAND 176 180 {ECO:0000244|PDB:3LCV}.
TURN 183 185 {ECO:0000244|PDB:3LCV}.
STRAND 193 197 {ECO:0000244|PDB:3LCV}.
HELIX 201 207 {ECO:0000244|PDB:3LCV}.
HELIX 211 218 {ECO:0000244|PDB:3LCV}.
STRAND 222 229 {ECO:0000244|PDB:3LCV}.
HELIX 240 255 {ECO:0000244|PDB:3LCV}.
STRAND 258 264 {ECO:0000244|PDB:3LCV}.
STRAND 267 273 {ECO:0000244|PDB:3LCV}.
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


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