ID W5U4J5_9ENTE Unreviewed; 250 AA.
AC W5U4J5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Neomycin phosphotransferase III {ECO:0000313|EMBL:AHH29397.1};
DE Flags: Fragment;
OS Enterococcus sp. EK_11/057.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1444642 {ECO:0000313|EMBL:AHH29397.1};
RN [1] {ECO:0000313|EMBL:AHH29397.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=EK_11/057 {ECO:0000313|EMBL:AHH29397.1};
RX PubMed=24194558;
RA Woegerbauer M., Zeinzinger J., Springer B., Hufnagl P., Indra A.,
RA Korschineck I., Hofrichter J., Kopacka I., Fuchs R., Steinwider J.,
RA Fuchs K., Nielsen K.M., Allerberger F.;
RT "Prevalence of the aminoglycoside phosphotransferase genes aph(3')-IIIa and
RT aph(3')-IIa in Escherichia coli, Enterococcus faecalis, Enterococcus
RT faecium, Pseudomonas aeruginosa, Salmonella enterica subsp. enterica and
RT Staphylococcus aureus isolates in Austria.";
RL J. Med. Microbiol. 63:210-217(2014).
CC -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC {ECO:0000256|ARBA:ARBA00006219}.
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DR EMBL; KF767705; AHH29397.1; -; Genomic_DNA.
DR AlphaFoldDB; W5U4J5; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR CDD; cd05150; APH; 1.
DR Gene3D; 3.90.1200.10; -; 1.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR024165; Kan/Strep_kinase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR21310; AMINOGLYCOSIDE PHOSPHOTRANSFERASE-RELATED-RELATED; 1.
DR PANTHER; PTHR21310:SF41; BLR5425 PROTEIN; 1.
DR Pfam; PF01636; APH; 1.
DR PIRSF; PIRSF000706; Kanamycin_kin; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000706-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000706-2};
KW Transferase {ECO:0000313|EMBL:AHH29397.1}.
FT DOMAIN 17..244
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000706-1"
FT BINDING 183
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000706-2"
FT BINDING 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000706-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AHH29397.1"
FT NON_TER 250
FT /evidence="ECO:0000313|EMBL:AHH29397.1"
SQ SEQUENCE 250 AA; 29300 MW; 93003E279CA7C7AB CRC64;
LIEKYRCVKD TEGMSPAKVY KLVGENENLY LKMTDSRYKG TTYDVEREKD MMLWLEGKLP
VPKVLHFERH DGWSNLLMSE ADGVLCSEEY EDEQSPEKII ELYAECIRLF HSIDISDCPY
TNSLDSRLAE LDYLLNNDLA DVDCENWEED TPFKDPRELY DFLKTEKPEE ELVFSHGDLG
DSNIFVKDGK VSGFIDLGRS GRADKWYDIA FCVRSIREDI GEEQYVELFF DLLGIKPDWE
KIKYYILLDE
//
