KKA7_CAMJU
ID KKA7_CAMJU Reviewed; 250 AA.
AC P14508;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Aminoglycoside 3'-phosphotransferase;
DE EC=2.7.1.95;
DE AltName: Full=APH(3')VII;
DE AltName: Full=Kanamycin kinase, type VII;
DE AltName: Full=Neomycin-kanamycin phosphotransferase type VII;
GN Name=aphA-7;
OS Campylobacter jejuni.
OG Plasmid.
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=197;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PS1178;
RX PubMed=2550983; DOI=10.1016/0147-619x(89)90035-8;
RA Tenover F.C., Gilbert T., O'Hara P.;
RT "Nucleotide sequence of a novel kanamycin resistance gene, aphA-7, from
RT Campylobacter jejuni and comparison to other kanamycin phosphotransferase
RT genes.";
RL Plasmid 22:52-58(1989).
CC -!- FUNCTION: Resistance to kanamycin and structurally-related
CC aminoglycosides, including amikacin.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + kanamycin A = ADP + H(+) + kanamycin 3'-phosphate;
CC Xref=Rhea:RHEA:24256, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57909, ChEBI:CHEBI:58214, ChEBI:CHEBI:456216;
CC EC=2.7.1.95;
CC -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC {ECO:0000305}.
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DR EMBL; M29953; AAA76822.1; -; Genomic_DNA.
DR PIR; A43623; A43623.
DR RefSeq; WP_063842175.1; NG_047447.1.
DR AlphaFoldDB; P14508; -.
DR SMR; P14508; -.
DR PRIDE; P14508; -.
DR KEGG; ag:AAA76822; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008910; F:kanamycin kinase activity; IEA:UniProtKB-EC.
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 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; SSF56112; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; ATP-binding; Kinase; Nucleotide-binding; Plasmid;
KW Transferase.
FT CHAIN 1..250
FT /note="Aminoglycoside 3'-phosphotransferase"
FT /id="PRO_0000204810"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 250 AA; 29688 MW; AF3B7ADDE85531EC CRC64;
MKYIDEIQIL GKCSEGMSPA EVYKCQLKNT VCYLKKIDDI FSKTTYSVKR EAEMMMWLSD
KLKVPDVIEY GVREHSEYLI MSELRGKHID CFIDHPIKYI ECLVNALHQL QAIDIRNCPF
SSKIDVRLKE LKYLLDNRIA DIDVSNWEDT TEFDDPMTLY QWLCENQPQE ELCLSHGDMS
ANFFVSHDGI YFYDLARCGV ADKWLDIAFC VREIREYYPD SDYEKFFFNM LGLEPDYKKI
NYYILLDEMF