ID A0A0W7WBL7_9MICO Unreviewed; 273 AA.
AC A0A0W7WBL7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Aminoglycoside phosphotransferase {ECO:0000313|EMBL:KUF08028.1};
GN ORFNames=AUL38_06665 {ECO:0000313|EMBL:KUF08028.1};
OS Leucobacter sp. G161.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=663704 {ECO:0000313|EMBL:KUF08028.1, ECO:0000313|Proteomes:UP000053012};
RN [1] {ECO:0000313|EMBL:KUF08028.1, ECO:0000313|Proteomes:UP000053012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G161 {ECO:0000313|EMBL:KUF08028.1,
RC ECO:0000313|Proteomes:UP000053012};
RA Ge S., Dong X.;
RT "High quality draft genome sequence of Leucobacter sp. G161, a distinct and
RT effective chromium reducer.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC {ECO:0000256|ARBA:ARBA00006219, ECO:0000256|PIRNR:PIRNR000706}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUF08028.1}.
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DR EMBL; LOHP01000034; KUF08028.1; -; Genomic_DNA.
DR RefSeq; WP_059059242.1; NZ_LOHP01000034.1.
DR AlphaFoldDB; A0A0W7WBL7; -.
DR STRING; 663704.AUL38_06665; -.
DR OrthoDB; 3806873at2; -.
DR Proteomes; UP000053012; Unassembled WGS sequence.
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 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 ECO:0000256|PIRNR:PIRNR000706};
KW ATP-binding {ECO:0000256|PIRNR:PIRNR000706};
KW Kinase {ECO:0000256|PIRNR:PIRNR000706};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000706-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000706-2};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000706};
KW Reference proteome {ECO:0000313|Proteomes:UP000053012};
KW Transferase {ECO:0000256|PIRNR:PIRNR000706, ECO:0000313|EMBL:KUF08028.1}.
FT DOMAIN 50..266
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
FT ACT_SITE 199
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000706-1"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000706-2"
FT BINDING 218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000706-2"
SQ SEQUENCE 273 AA; 28995 MW; 4E00288B8E6EF118 CRC64;
MSDFRLPLAQ IPQGPVATPP TVRELTAGRA LEAVWVNGLG GLTFRDAGPG DGARFVKWVA
AGTPEIDLAA EAARLRWAGQ HGAVAPTVIE QGTNAHGSWL ITAALAGESA VSPRWIAEPE
TAARAIGAGL RLLHDTLPVV SCPYRWDVTT RAAQFEQRIR AGAGPADWAP AYRGLSVARV
REILRESPAV ADPVVCHGDP CAPNTLIGGD GTFAGHVDLG DLGVGDRWAD LAVAAWSTEW
NYGPGFDEHV YEGYGVTADA ERIAFYRLLW EVS
//
