ID   STRA_STRGA              Reviewed;         307 AA.
AC   P18622;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Streptomycin 6-kinase;
DE            EC=2.7.1.72;
DE   AltName: Full=APH(6);
DE   AltName: Full=Streptidine kinase;
DE   AltName: Full=Streptomycin 6-phosphotransferase;
GN   Name=sph;
OS   Streptomyces glaucescens.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 40716 / ETH 22794 / Tue 49;
RX   PubMed=3039305; DOI=10.1007/bf00330442;
RA   Voegtli M., Huetter R.;
RT   "Characterisation of the hydroxystreptomycin phosphotransferase gene (sph)
RT   of Streptomyces glaucescens: nucleotide sequence and promoter analysis.";
RL   Mol. Gen. Genet. 208:195-203(1987).
CC   -!- FUNCTION: The aminoglycoside phosphotransferases achieve inactivation
CC       of their antibiotic substrates by phosphorylation.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + streptomycin = ADP + H(+) + streptomycin 6-phosphate;
CC         Xref=Rhea:RHEA:22268, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57787, ChEBI:CHEBI:58007, ChEBI:CHEBI:456216;
CC         EC=2.7.1.72;
CC   -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC       {ECO:0000305}.
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DR   EMBL; X05648; CAA29136.1; -; Genomic_DNA.
DR   PIR; S07039; KISM6C.
DR   RefSeq; WP_052413554.1; NZ_CP009438.1.
DR   AlphaFoldDB; P18622; -.
DR   SMR; P18622; -.
DR   STRING; 1907.SGLAU_01165; -.
DR   KEGG; ag:CAA29136; -.
DR   eggNOG; COG3570; Bacteria.
DR   OMA; GDRMLHW; -.
DR   OrthoDB; 1457558at2; -.
DR   GO; GO:0050300; F:aminoglycoside 6-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   GO; GO:0019748; P:secondary metabolic process; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR006748; NH2Glyco/OHUrea_AB-resist_kin.
DR   Pfam; PF04655; APH_6_hur; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; ATP-binding; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..307
FT                   /note="Streptomycin 6-kinase"
FT                   /id="PRO_0000204816"
FT   ACT_SITE        201
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         133..145
FT                   /ligand="streptomycin"
FT                   /ligand_id="ChEBI:CHEBI:58007"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   307 AA;  33154 MW;  C3BB4309C34B5F7D CRC64;
     MSTSKLVEIP EPLAASYARA FGEEGQAWIA ALPALVEELL DRWELTADGA SASGEASLVL
     PVLRTDGTRA VLKLQLPREE TSAAITGLRT WNGHGVVRLL DHDPRSSTML LERLDASRTL
     ASVEDDDAAM GVLAGLLARL VSVPAPRGLR GLGDIAGAML EEVPRAVAAL ADPADRRLLN
     DWASAVAELV GEPGDRMLHW DLHYGNVLAA EREPWLAIDP EPLAGDPGFD LWPALDSRWD
     DIVAQRDVVR VVRRRFDLLT EVLGLDRARA AGWTYGRLLQ NALWDIEDGS AALDPAAVTL
     AQALRGH