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STR_KLEPN
ID   STR_KLEPN               Reviewed;         266 AA.
AC   P13082;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Streptomycin 3''-kinase;
DE            EC=2.7.1.87;
DE   AltName: Full=Streptomycin 3''-phosphotransferase;
DE            Short=SPH;
GN   Name=str;
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3889831; DOI=10.1093/nar/13.1.195;
RA   Mazodier P., Cossart P., Giraud E., Gasser F.;
RT   "Completion of the nucleotide sequence of the central region of Tn5
RT   confirms the presence of three resistance genes.";
RL   Nucleic Acids Res. 13:195-205(1985).
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   -!- MISCELLANEOUS: This enzyme is encoded by the kanamycin and neomycin
CC       resistance transposon Tn5.
CC   -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC       {ECO:0000305}.
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DR   EMBL; U00004; AAA73392.1; -; Unassigned_DNA.
DR   EMBL; X01702; CAA25854.1; -; Genomic_DNA.
DR   RefSeq; WP_011666520.1; NZ_VABX01000066.1.
DR   RefSeq; YP_788128.1; NC_008460.1.
DR   AlphaFoldDB; P13082; -.
DR   SMR; P13082; -.
DR   KEGG; ag:CAA25854; -.
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: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; Transposable element.
FT   CHAIN           1..266
FT                   /note="Streptomycin 3''-kinase"
FT                   /id="PRO_0000204814"
FT   ACT_SITE        154
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   266 AA;  29066 MW;  30A9DA5D0E1A826C CRC64;
     MERWRLLRDG ELLTTHSSWI LPVRQGDMPA MLKVARIPDE EAGYRLLTWW DGQGAARVFA
     SAAGALLMER ASGAGDLAQI AWSGQDDEAC RILCDTAARL HAPRSGPPPD LHPLQEWFQP
     LFRLAAEHAA LAPAASVARQ LLAAPREVCP LHGDLHHENV LDFGDRGWLA IDPHGLLGER
     TFDYANIFTN PDLSDPGRPL AILPGRLEAR LSIVVATTGF EPERLLRWII AWTGLSAAWF
     IGDGDGEGEG AAIDLAVNAM ARRLLD
 
 
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