P05057 (KANU_STAAU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Kanamycin nucleotidyltransferase
Short name=Neo(R)
EC=2.7.7.-

Gene names

Name:	knt
Synonyms:	kan

Encoded on

Plasmid pUB110

Organism

Staphylococcus aureus

Taxonomic identifier

1280 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	253 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Inactivates the antibiotic kanamycin by catalyzing the transfer of a nucleotidyl group from nucleoside triphosphates such as ATP to the 4'-hydroxyl group of the aminoglycoside.
Subunit structure	Homodimer.

Ontologies

Keywords
Biological process	Antibiotic resistance
Molecular function	Transferase
Technical term	3D-structure Direct protein sequencing Plasmid
Gene Ontology (GO)
Biological process	response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	nucleotidyltransferase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 253

253

Kanamycin nucleotidyltransferase

PRO_0000068568

Secondary structure

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253

Helix Strand Turn

Details...

Helix

9 – 27

19

Helix

28 – 30

3

Beta strand

31 – 37

7

Helix

38 – 42

5

Turn

43

1

Turn

47 – 48

2

Beta strand

51 – 59

9

Turn

60 – 61

2

Beta strand

63 – 69

7

Beta strand

74 – 81

8

Helix

82 – 89

8

Turn

90

1

Turn

94 – 95

2

Helix

96 – 99

4

Helix

100 – 103

4

Beta strand

107 – 114

8

Helix

115 – 124

10

Helix

128 – 141

14

Turn

142

1

Helix

143 – 156

14

Helix

159 – 161

3

Helix

162 – 181

20

Turn

182

1

Beta strand

186 – 190

5

Helix

191 – 195

5

Turn

196 – 197

2

Beta strand

198 – 200

3

Turn

203 – 204

2

Helix

205 – 214

10

Turn

215

1

Helix

220 – 241

22

Turn

242

1

Sequences

	Sequence		Length	Mass (Da)
	P05057 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: 9CB3D60E72A45DC6	FASTA	253	28,798
	10 20 30 40 50 60 MNGPIIMTRE ERMKIVHEIK ERILDKYGDD VKAIGVYGSL GRQTDGPYSD IEMMCVMSTE 70 80 90 100 110 120 EAEFSHEWTT GEWKVEVNFD SEEILLDYAS QVESDWPLTH GQFFSILPIY DSGGYLEKVY 130 140 150 160 170 180 QTAKSVEAQT FHDAICALIV EELFEYAGKW RNIRVQGPTT FLPSLTVQVA MAGAMLIGLH 190 200 210 220 230 240 HRICYTTSAS VLTEAVKQSD LPSGYDHLCQ FVMSGQLSDS EKLLESLENF WNGIQEWTER 250 HGYIVDVSKR IPF

References

[1]	"Complete nucleotide sequences of Bacillus plasmids pUB110dB, pRBH1 and its copy mutants." Mueller R.E., Ano T., Imanaka T., Aiba S. Mol. Gen. Genet. 202:169-171(1986) [PubMed: 3007933] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Enzymatic and nucleotide sequence studies of a kanamycin-inactivating enzyme encoded by a plasmid from thermophilic bacilli in comparison with that encoded by plasmid pUB110." Matsumura M., Katakura Y., Imanaka T., Aiba S. J. Bacteriol. 160:413-420(1984) [PubMed: 6090428] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-7.
[3]	"Nucleotide sequence and physical map of kanamycin-resistant plasmid pUB110 from Staphylococcus aureus." Bashkirov V.I., Mil'Shina N.V., Prozorov A.A. Genetika 22:1081-1092(1986) [PubMed: 3744038] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"The nucleotide sequence of pUB110: some salient features in relation to replication and its regulation." McKenzie T., Hoshino T., Tanaka T., Sueoka N. Plasmid 15:93-103(1986) [PubMed: 3010356] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Correction. A revision of the nucleotide sequence and functional map of pUB110." McKenzie T., Hoshino T., Tanaka T., Sueoka N. Plasmid 17:83-85(1987) [PubMed: 3033723] [Abstract] Cited for: SEQUENCE REVISION.
[6]	"Molecular structure of kanamycin nucleotidyltransferase determined to 3.0-A resolution." Sakon J., Liao H.H., Kanikula A.M., Benning M.M., Rayment I., Holden H.M. Biochemistry 32:11977-11984(1993) [PubMed: 8218273] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[7]	"Structural investigation of the antibiotic and ATP-binding sites in kanamycin nucleotidyltransferase." Pedersen L.C., Benning M.M., Holden H.M. Biochemistry 34:13305-13311(1995) [PubMed: 7577914] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X03408 Genomic DNA. Translation: CAA27142.1.
M37273 Genomic DNA. Translation: AAA98214.1.
M19465 Genomic DNA. Translation: AAA88361.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KAN	X-ray	3.00	A/B	1-253	[»]
1KNY	X-ray	2.50	A/B	1-253	[»]

ProteinModelPortal

P05057.

SMR

P05057. Positions 1-253.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

ProtClustDB

CLSK861689.

Family and domain databases

InterPro

IPR012481. KNTase_C.
IPR002934. Nucleotidyltransferase.
[Graphical view]

Pfam

PF07827. KNTase_C. 1 hit.
PF01909. NTP_transf_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB01172. Kanamycin.

Entry information

Entry name

KANU_STAAU

Accession

Primary (citable) accession number: P05057

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	November 30, 2010
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program