General Information of the Molecule (ID: Mol01092)
Name
Streptomycin 3''-kinase (APHE) ,Streptomyces griseus
Synonyms
Streptomycin 3''-phosphotransferase; Streptomycin 6-kinase; Streptomycin 6-phosphotransferase
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Molecule Type
Protein
Gene Name
aphE
Sequence
MSDHPGPGAVTPELFGVGGDWLAVTAGESGASVFRAADATRYAKCVPAADAAGLEAERDR
IAWLSGQGVPGPRVLDWYAGDAGACLVTRAVPGVPADRVGADDLRTAWGAVADAVRRLHE
VPVASCPFRRGLDSVVDAARDVVARGAVHPEFLPVEQRLVPPAELLARLTGELARRRDQE
AADTVVCHGDLCLPNIVLHPETLEVSGFIDLGRLGAADRHADLALLLANARETWVDEERA
RFADAAFAERYGIAPDPERLRFYLHLDPLTWG
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Function
The aminoglycoside phosphotransferases achieve inactivation of their antibiotic substrates by phosphorylation.
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Uniprot ID
APHE_STRGR
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Kingdom: N.A.
Phylum: Actinobacteria
Class: Actinomycetia
Order: Streptomycetales
Family: Streptomycetaceae
Genus: Streptomyces
Species: Streptomyces griseus
Type(s) of Resistant Mechanism of This Molecule
  DISM: Drug Inactivation by Structure Modification
Drug Resistance Data Categorized by Drug
Approved Drug(s)
1 drug(s) in total
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Streptomycin
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Drug Resistance Data Categorized by Their Corresponding Mechanisms
       Drug Inactivation by Structure Modification (DISM) Click to Show/Hide
Disease Class: Streptomyces griseus infection [1]
Resistant Disease Streptomyces griseus infection [ICD-11: 1C43.7]
Resistant Drug Streptomycin
Molecule Alteration Expression
Inherence
Experimental Note Discovered Using In-vivo Testing Model
In Vitro Model Streptomyces griseus strain ATCC 12475 1911
Mechanism Description The aminoglycoside phosphotransferases are prokaryotic antibiotic resistance proteins that achieve inactivation of their antibiotic substrates by phosphorylation. To assist in our structure/function investigations of this group of kinases a gene encoding a streptomycin phosphotransferase (aphE) was cloned from the chromosomal DNA of the streptomycin producing Streptomyces griseus ATCC 12475 by the polymerase chain reaction (PCR).
References
Ref 1 PCR cloning of a streptomycin phosphotransferase (aphE) gene from Streptomyces griseus ATCC 12475. Nucleic Acids Res. 1990 Aug 11;18(15):4615. doi: 10.1093/nar/18.15.4615.

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