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