[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=N2-3-11; DOI=10.1093/nar/15.19.8041; PubMed=3118332 [NCBI, ExPASy, EBI, Israel, Japan] Distler J., Ebert A., Mansouri K., Pissowotzki K., Stockmann M., Piepersberg W.; "Gene cluster for streptomycin biosynthesis in Streptomyces griseus: nucleotide sequence of three genes and analysis of transcriptional activity."; Nucleic Acids Res. 15:8041-8056(1987).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 23345 / DSM 40236 / IFO 12875 / JCM 4644 / NCIMB 13023; DOI=10.1093/nar/15.4.1819; PubMed=3029728 [NCBI, ExPASy, EBI, Israel, Japan] Tohyama H., Okami Y., Umezawa H.; "Nucleotide sequence of the streptomycinphosphotransferase and amidinotransferase genes from Streptomyces griseus."; Nucleic Acids Res. 15:1819-1833(1987).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1007/BF00330443; PubMed=3039306 [NCBI, ExPASy, EBI, Israel, Japan] Distler J., Braun C., Ebert A., Piepersberg W.; "Gene cluster for streptomycin biosynthesis in Streptomyces griseus: analysis of a central region including the major resistance gene."; Mol. Gen. Genet. 208:204-210(1987).

Comments

FUNCTION: The aminoglycoside phosphotransferases achieve inactivation of their antibiotic substrates by phosphorylation.
CATALYTIC ACTIVITY: ATP + streptomycin = ADP + streptomycin 6-phosphate.
SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Y00459; CAA68516.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X05045; CAA28717.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X05647; CAA29134.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A26674; A26674.
S06355; KISM6G.

3D structure databases

ModBase

P08077.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-14016; -.

Ontologies

GO:0050300;	Molecular function: aminoglycoside 6-kinase activity (inferred from electronic annotation from EC).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006468;	Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
GO:0046677;	Biological process: response to antibiotic (inferred from electronic annotation from UniProtKB-KW).
GO:0019748;	Biological process: secondary metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR006748; APH_6_hur.
Graphical view of domain structure.

Pfam

PF04655; APH_6_hur; 1.
Pfam graphical view of domain structure.

Other

ProtoNet

P08077.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Antibiotic resistance; ATP-binding; Kinase; Nucleotide-binding; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 307`	`307`	`Streptomycin 6-kinase.`	`PRO_0000204815`
`REGION`	`133 145`	`13`	`Aminoglycoside binding (By similarity).`
`ACT_SITE`	`201 201`		`By similarity.`
`VARIANT`	`34 39`	`6`	`ALVARC -> GSRRAI (in strain: ISP 5236).`
`VARIANT`	`115 120`	`6`	`DGSRTL -> GRFADV (in strain: ISP 5236).`
`VARIANT`	`181 188`	`8`	`GWASAVAE -> AVGVGREP (in strain: ISP 5236).`
`VARIANT`	`225 225`	`1`	`G -> A (in strain: ISP 5236).`
`VARIANT`	`262 262`	`1`	`S -> A (in strain: ISP 5236).`

Sequence information

Length: 307 AA [This is the length of the unprocessed precursor]

Molecular weight: 33244 Da [This is the MW of the unprocessed precursor]

CRC64: 382DFD60DF4028AA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSSSDHIHVP DGLAESYSRS GGEEGRAWIA GLPALVARCV DRWELKRDGG VRSGEASLVV 

        70         80         90        100        110        120 
PVLRADGTRA ALKLQMPREE TTAALIGLRA WGGDGMVRLL DHDEESSTML LERLDGSRTL 

       130        140        150        160        170        180 
ASVEDDDEAM GVLAGLLNRL HSVPAPPGLR GLGEIAGAMV EEVPSAVDSL ADPEDRSRLR 

       190        200        210        220        230        240 
GWASAVAELV GEPGDRVLHW DLHYENVLAA EREPWLAIDP EPLVGDPGFD LWPALDTGWE 

       250        260        270        280        290        300 
RIEATGDARR VVRRRFDLLT ESLELDRGRA AGWTLARLLQ NTLWDIEDGL TAIAPSQIAV 


AEALAKP

P08077 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools