ID   KANU_BACSP              Reviewed;         253 AA.
AC   P05058;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Kanamycin nucleotidyltransferase;
DE            EC=2.7.7.-;
GN   Name=knt; Synonyms=kan;
OS   Bacillus sp.
OG   Plasmid pRBH1, and Plasmid pTB913.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1409;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pRBH1;
RX   PubMed=3007933; DOI=10.1007/bf00330534;
RA   Mueller R.E., Ano T., Imanaka T., Aiba S.;
RT   "Complete nucleotide sequences of Bacillus plasmids pUB110dB, pRBH1 and its
RT   copy mutants.";
RL   Mol. Gen. Genet. 202:169-171(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-7.
RC   PLASMID=pTB913;
RX   PubMed=6090428; DOI=10.1128/jb.160.1.413-420.1984;
RA   Matsumura M., Katakura Y., Imanaka T., Aiba S.;
RT   "Enzymatic and nucleotide sequence studies of a kanamycin-inactivating
RT   enzyme encoded by a plasmid from thermophilic bacilli in comparison with
RT   that encoded by plasmid pUB110.";
RL   J. Bacteriol. 160:413-420(1984).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pTB913;
RX   PubMed=2677995; DOI=10.1093/nar/17.18.7283;
RA   van der Lelie D., Bron S., Venema G., Oskam L.;
RT   "Similarity of minus origins of replication and flanking open reading
RT   frames of plasmids pUB110, pTB913 and pMV158.";
RL   Nucleic Acids Res. 17:7283-7294(1989).
CC   -!- FUNCTION: Inactivates the antibiotic kanamycin by catalyzing the
CC       transfer of a nucleotidyl group from nucleoside triphosphates such as
CC       ATP to the 4'-hydroxyl group of the aminoglycoside.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA33715.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; K02551; AAA92254.1; -; Genomic_DNA.
DR   EMBL; X03409; CAA27144.1; -; Genomic_DNA.
DR   EMBL; X15670; CAA33715.1; ALT_INIT; Genomic_DNA.
DR   PIR; B24456; B24456.
DR   PDB; 6P01; X-ray; 1.89 A; A/B=1-253.
DR   PDB; 6P04; X-ray; 2.30 A; A/B=1-253.
DR   PDB; 6P06; X-ray; 2.30 A; A/B=1-253.
DR   PDB; 6P08; X-ray; 2.27 A; A/D=1-253.
DR   PDBsum; 6P01; -.
DR   PDBsum; 6P04; -.
DR   PDBsum; 6P06; -.
DR   PDBsum; 6P08; -.
DR   AlphaFoldDB; P05058; -.
DR   SMR; P05058; -.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.460.10; -; 1.
DR   InterPro; IPR012481; KNTase_C.
DR   InterPro; IPR043519; NT_sf.
DR   Pfam; PF07827; KNTase_C; 1.
DR   SUPFAM; SSF81301; SSF81301; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic resistance; Direct protein sequencing; Plasmid;
KW   Transferase.
FT   CHAIN           1..253
FT                   /note="Kanamycin nucleotidyltransferase"
FT                   /id="PRO_0000068567"
FT   HELIX           9..27
FT                   /evidence="ECO:0007829|PDB:6P01"
FT   HELIX           28..30
FT                   /evidence="ECO:0007829|PDB:6P01"
FT   STRAND          31..37
FT                   /evidence="ECO:0007829|PDB:6P01"
FT   HELIX           38..41
FT                   /evidence="ECO:0007829|PDB:6P01"
FT   STRAND          51..59
FT                   /evidence="ECO:0007829|PDB:6P01"
FT   STRAND          63..69
FT                   /evidence="ECO:0007829|PDB:6P01"
FT   STRAND          74..81
FT                   /evidence="ECO:0007829|PDB:6P01"
FT   HELIX           82..89
FT                   /evidence="ECO:0007829|PDB:6P01"
FT   HELIX           96..99
FT                   /evidence="ECO:0007829|PDB:6P01"
FT   HELIX           100..104
FT                   /evidence="ECO:0007829|PDB:6P01"
FT   STRAND          107..114
FT                   /evidence="ECO:0007829|PDB:6P01"
FT   HELIX           115..124
FT                   /evidence="ECO:0007829|PDB:6P01"
FT   HELIX           128..141
FT                   /evidence="ECO:0007829|PDB:6P01"
FT   HELIX           143..156
FT                   /evidence="ECO:0007829|PDB:6P01"
FT   HELIX           159..161
FT                   /evidence="ECO:0007829|PDB:6P01"
FT   HELIX           162..181
FT                   /evidence="ECO:0007829|PDB:6P01"
FT   HELIX           188..190
FT                   /evidence="ECO:0007829|PDB:6P01"
FT   HELIX           191..196
FT                   /evidence="ECO:0007829|PDB:6P01"
FT   STRAND          198..200
FT                   /evidence="ECO:0007829|PDB:6P01"
FT   HELIX           205..214
FT                   /evidence="ECO:0007829|PDB:6P01"
FT   HELIX           220..241
FT                   /evidence="ECO:0007829|PDB:6P01"
SQ   SEQUENCE   253 AA;  28825 MW;  9CA14603E2BB5DC6 CRC64;
     MNGPIIMTRE ERMKIVHEIK ERILDKYGDD VKAIGVYGSL GRQTDGPYSD IEMMCVMSTE
     EAEFSHEWTT GEWKVEVNFD SEEILLDYAS QVESDWPLTH GQFFSILPIY DSGGYLEKVY
     QTAKSVEAQK FHDAICALIV EELFEYAGKW RNIRVQGPTT FLPSLTVQVA MAGAMLIGLH
     HRICYTTSAS VLTEAVKQSD LPSGYDHLCQ FVMSGQLSDS EKLLESLENF WNGIQEWTER
     HGYIVDVSKR IPF