Molecule Information

General Information of the Molecule (ID: Mol00748)

• Name: 16S rRNA (adenine(1408)-N(1))-methyltransferase (KAMB) ,Streptoalloteichus tenebrarius
• Synonyms: 16S rRNA m1A1408 methyltransferase; Kanamycin-apramycin resistance methylase
• Molecule Type: Protein
• Gene Name: kamB
• Sequence:
  MRRVVGKRVQEFSDAEFEQLRSQYDDVVLDVGTGDGKHPYKVARQNPSRLVVALDADKSR
  MEKISAKAAAKPAKGGLPNLLYLWATAERLPPLSGVGELHVLMPWGSLLRGVLGSSPEML
  RGMAAVCRPGASFLVALNLHAWRPSVPEVGEHPEPTPDSADEWLAPRYAEAGWKLADCRY
  LEPEEVAGLETSWTRRLHSSRDRFDVLALTGTISP
• Function: Specifically methylates the N(1) position of adenine 1408 in 16S rRNA. Confers resistance to various aminoglycosides, including kanamycin, neomycin and apramycin.
• Uniprot ID: KAMB_STRSD

Kingdom: N.A.
Phylum: Actinobacteria
Class: Actinomycetia
Order: Pseudonocardiales
Family: Pseudonocardiaceae
Genus: Streptoalloteichus
Species: Streptoalloteichus tenebrarius

Type(s) of Resistant Mechanism of This Molecule

  ADTT: Aberration of the Drug's Therapeutic Target

Drug Resistance Data Categorized by Drug

Approved Drug(s) 2 drug(s) in total

Framycetin

Drug Resistance Data Categorized by Their Corresponding Mechanisms

Aberration of the Drug's Therapeutic Target (ADTT)

Disease Class: Bacterial infection [1], [2]

• Resistant Disease: Bacterial infection [ICD-11: 1A00-1C4Z]
• Resistant Drug: Framycetin
• Molecule Alteration: Expression; Up-regulation
• Experimental Note: Identified from the Human Clinical Data
• In Vitro Model: Escherichia coli BL21(DE3); 469008
• Experiment for Molecule Alteration: Whole genome sequence assay
• Experiment for Drug Resistance: MIC assay
• Mechanism Description: The 16S ribosomal RNA methyltransferase enzymes that modify nucleosides in the drug binding site to provide self-resistance in aminoglycoside-producing micro-organisms have been proposed to comprise two distinct groups of S-adenosyl-l-methionine (SAM)-dependent RNA enzymes, namely the kgm and kam families.

Kanamycin

Drug Resistance Data Categorized by Their Corresponding Mechanisms

Aberration of the Drug's Therapeutic Target (ADTT)

Disease Class: Bacterial infection [1], [2]

• Resistant Disease: Bacterial infection [ICD-11: 1A00-1C4Z]
• Resistant Drug: Kanamycin
• Molecule Alteration: Expression; Up-regulation
• Experimental Note: Identified from the Human Clinical Data
• In Vitro Model: Escherichia coli BL21(DE3); 469008
• Experiment for Molecule Alteration: Whole genome sequence assay
• Experiment for Drug Resistance: MIC assay
• Mechanism Description: The 16S ribosomal RNA methyltransferase enzymes that modify nucleosides in the drug binding site to provide self-resistance in aminoglycoside-producing micro-organisms have been proposed to comprise two distinct groups of S-adenosyl-l-methionine (SAM)-dependent RNA enzymes, namely the kgm and kam families.

Clinical Trial Drug(s) 1 drug(s) in total

Apramycin

Drug Resistance Data Categorized by Their Corresponding Mechanisms

Aberration of the Drug's Therapeutic Target (ADTT)

Disease Class: Bacterial infection [1], [2]

• Resistant Disease: Bacterial infection [ICD-11: 1A00-1C4Z]
• Resistant Drug: Apramycin
• Molecule Alteration: Expression; Up-regulation
• Experimental Note: Identified from the Human Clinical Data
• In Vitro Model: Escherichia coli BL21(DE3); 469008
• Experiment for Molecule Alteration: Whole genome sequence assay
• Experiment for Drug Resistance: MIC assay
• Mechanism Description: The 16S ribosomal RNA methyltransferase enzymes that modify nucleosides in the drug binding site to provide self-resistance in aminoglycoside-producing micro-organisms have been proposed to comprise two distinct groups of S-adenosyl-l-methionine (SAM)-dependent RNA enzymes, namely the kgm and kam families.

References

• Ref 1: 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. 2009 Sep;37(16):5420-31. doi: 10.1093/nar/gkp575. Epub 2009 Jul 9.
• Ref 2: Expansion of the aminoglycoside-resistance 16S rRNA (m(1)A1408) methyltransferase family: expression and functional characterization of four hypothetical enzymes of diverse bacterial origin. Biochim Biophys Acta. 2014 Sep;1844(9):1648-55. doi: 10.1016/j.bbapap.2014.06.012. Epub 2014 Jun 22.