KANU_STAAU
ID KANU_STAAU Reviewed; 253 AA.
AC P05057;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Kanamycin nucleotidyltransferase;
DE Short=Neo(R);
DE EC=2.7.7.-;
GN Name=knt; Synonyms=kan;
OS Staphylococcus aureus.
OG Plasmid pUB110.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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.
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].
RX PubMed=3744038;
RA Bashkirov V.I., Mil'Shina N.V., Prozorov A.A.;
RT "Nucleotide sequence and physical map of kanamycin-resistant plasmid pUB110
RT from Staphylococcus aureus.";
RL Genetika 22:1081-1092(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3010356; DOI=10.1016/0147-619x(86)90046-6;
RA McKenzie T., Hoshino T., Tanaka T., Sueoka N.;
RT "The nucleotide sequence of pUB110: some salient features in relation to
RT replication and its regulation.";
RL Plasmid 15:93-103(1986).
RN [5]
RP SEQUENCE REVISION.
RX PubMed=3033723; DOI=10.1016/0147-619x(87)90015-1;
RA McKenzie T., Hoshino T., Tanaka T., Sueoka N.;
RT "Correction. A revision of the nucleotide sequence and functional map of
RT pUB110.";
RL Plasmid 17:83-85(1987).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=8218273; DOI=10.1021/bi00096a006;
RA Sakon J., Liao H.H., Kanikula A.M., Benning M.M., Rayment I., Holden H.M.;
RT "Molecular structure of kanamycin nucleotidyltransferase determined to 3.0-
RT A resolution.";
RL Biochemistry 32:11977-11984(1993).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=7577914; DOI=10.1021/bi00041a005;
RA Pedersen L.C., Benning M.M., Holden H.M.;
RT "Structural investigation of the antibiotic and ATP-binding sites in
RT kanamycin nucleotidyltransferase.";
RL Biochemistry 34:13305-13311(1995).
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.
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DR EMBL; X03408; CAA27142.1; -; Genomic_DNA.
DR EMBL; M37273; AAA98214.1; -; Genomic_DNA.
DR EMBL; M19465; AAA88361.1; -; Genomic_DNA.
DR RefSeq; NP_040433.1; NC_001384.1.
DR RefSeq; WP_001014230.1; NG_047373.1.
DR RefSeq; YP_006937662.1; NC_013320.1.
DR RefSeq; YP_006938491.1; NC_013342.1.
DR PDB; 1KAN; X-ray; 3.00 A; A/B=1-253.
DR PDB; 1KNY; X-ray; 2.50 A; A/B=1-253.
DR PDB; 6NLT; X-ray; 1.90 A; A/B=1-253.
DR PDB; 6UN8; X-ray; 1.65 A; A/B=1-253.
DR PDBsum; 1KAN; -.
DR PDBsum; 1KNY; -.
DR PDBsum; 6NLT; -.
DR PDBsum; 6UN8; -.
DR AlphaFoldDB; P05057; -.
DR SMR; P05057; -.
DR DrugBank; DB01172; Kanamycin.
DR KEGG; ag:AAA88361; -.
DR EvolutionaryTrace; P05057; -.
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_0000068568"
FT HELIX 9..27
FT /evidence="ECO:0007829|PDB:6UN8"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:6UN8"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:6UN8"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:6UN8"
FT STRAND 51..59
FT /evidence="ECO:0007829|PDB:6UN8"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:6UN8"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:6UN8"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:6UN8"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:6UN8"
FT HELIX 100..104
FT /evidence="ECO:0007829|PDB:6UN8"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:6UN8"
FT HELIX 115..124
FT /evidence="ECO:0007829|PDB:6UN8"
FT HELIX 128..141
FT /evidence="ECO:0007829|PDB:6UN8"
FT HELIX 143..156
FT /evidence="ECO:0007829|PDB:6UN8"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:6UN8"
FT HELIX 162..181
FT /evidence="ECO:0007829|PDB:6UN8"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:6UN8"
FT HELIX 191..196
FT /evidence="ECO:0007829|PDB:6UN8"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:6UN8"
FT HELIX 205..214
FT /evidence="ECO:0007829|PDB:6UN8"
FT HELIX 220..241
FT /evidence="ECO:0007829|PDB:6UN8"
SQ SEQUENCE 253 AA; 28798 MW; 9CB3D60E72A45DC6 CRC64;
MNGPIIMTRE ERMKIVHEIK ERILDKYGDD VKAIGVYGSL GRQTDGPYSD IEMMCVMSTE
EAEFSHEWTT GEWKVEVNFD SEEILLDYAS QVESDWPLTH GQFFSILPIY DSGGYLEKVY
QTAKSVEAQT FHDAICALIV EELFEYAGKW RNIRVQGPTT FLPSLTVQVA MAGAMLIGLH
HRICYTTSAS VLTEAVKQSD LPSGYDHLCQ FVMSGQLSDS EKLLESLENF WNGIQEWTER
HGYIVDVSKR IPF
