APHE_STRGR
ID APHE_STRGR Reviewed; 272 AA.
AC P18150;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Streptomycin 3''-kinase;
DE EC=2.7.1.87;
DE AltName: Full=Streptomycin 3''-phosphotransferase;
DE AltName: Full=Streptomycin 6-kinase;
DE AltName: Full=Streptomycin 6-phosphotransferase;
GN Name=aphE;
OS Streptomyces griseus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 12475 / U-76;
RX PubMed=2167474; DOI=10.1093/nar/18.15.4615;
RA Trower M.K., Clark K.G.;
RT "PCR cloning of a streptomycin phosphotransferase (aphE) gene from
RT Streptomyces griseus ATCC 12475.";
RL Nucleic Acids Res. 18:4615-4615(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=N2-3-11;
RX PubMed=2844130; DOI=10.1007/bf00425160;
RA Heinzel P., Werbitzky O., Distler J., Piepersberg W.;
RT "A second streptomycin resistance gene from Streptomyces griseus codes for
RT streptomycin-3''-phosphotransferase. Relationships between antibiotic and
RT protein kinases.";
RL Arch. Microbiol. 150:184-192(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2821169; DOI=10.1099/00221287-134-5-1391;
RA Shinkawa H., Sugiyama M., Nimi O.;
RT "The nucleotide sequence of a streptomycin streptomycin phosphotransferase
RT (streptomycin kinase) gene from a streptomycin producer.";
RL J. Gen. Microbiol. 133:1289-1296(1987).
RN [4]
RP ERRATUM OF PUBMED:2821169.
RA Shinkawa H., Sugiyama M., Nimi O.;
RL J. Gen. Microbiol. 134:1391-1394(1988).
CC -!- FUNCTION: The aminoglycoside phosphotransferases achieve inactivation
CC of their antibiotic substrates by phosphorylation.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + streptomycin = ADP + H(+) + streptomycin 3''-phosphate;
CC Xref=Rhea:RHEA:18377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57482, ChEBI:CHEBI:58007, ChEBI:CHEBI:456216;
CC EC=2.7.1.87;
CC -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X53527; CAA37605.1; -; Genomic_DNA.
DR EMBL; M37378; AAA26700.1; -; Genomic_DNA.
DR EMBL; M16482; AAA26815.1; -; Genomic_DNA.
DR PIR; A46563; A46563.
DR PIR; JL0031; JL0031.
DR RefSeq; WP_063840676.1; NZ_JAAGMI010001012.1.
DR RefSeq; WP_063840677.1; NG_047410.1.
DR AlphaFoldDB; P18150; -.
DR SMR; P18150; -.
DR KEGG; ag:AAA26815; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050299; F:streptomycin 3''-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR CDD; cd05150; APH; 1.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR024165; Kan/Strep_kinase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR Pfam; PF01636; APH; 1.
DR PIRSF; PIRSF000706; Kanamycin_kin; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; ATP-binding; Kinase; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..272
FT /note="Streptomycin 3''-kinase"
FT /id="PRO_0000204801"
FT ACT_SITE 190
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT CONFLICT 51
FT /note="A -> P (in Ref. 2; AAA26700)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="V -> A (in Ref. 2; AAA26700)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 272 AA; 29060 MW; 71151C15DDA0E392 CRC64;
MSDHPGPGAV TPELFGVGGD WLAVTAGESG ASVFRAADAT RYAKCVPAAD AAGLEAERDR
IAWLSGQGVP GPRVLDWYAG DAGACLVTRA VPGVPADRVG ADDLRTAWGA VADAVRRLHE
VPVASCPFRR GLDSVVDAAR DVVARGAVHP EFLPVEQRLV PPAELLARLT GELARRRDQE
AADTVVCHGD LCLPNIVLHP ETLEVSGFID LGRLGAADRH ADLALLLANA RETWVDEERA
RFADAAFAER YGIAPDPERL RFYLHLDPLT WG
