ID Q5FJE9_LACAC Unreviewed; 260 AA.
AC Q5FJE9;
DT 01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Kanamycin kinase {ECO:0000313|EMBL:AAV43175.1};
DE EC=2.7.1.95 {ECO:0000313|EMBL:AAV43175.1};
GN OrderedLocusNames=LBA1348 {ECO:0000313|EMBL:AAV43175.1};
OS Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=272621 {ECO:0000313|Proteomes:UP000006381};
RN [1] {ECO:0000313|EMBL:AAV43175.1, ECO:0000313|Proteomes:UP000006381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700396 / NCK56 / N2 / NCFM
RC {ECO:0000313|Proteomes:UP000006381};
RX PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA Hamrick A., Cano R., Klaenhammer T.R.;
RT "Complete genome sequence of the probiotic lactic acid bacterium
RT Lactobacillus acidophilus NCFM.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
CC -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC {ECO:0000256|ARBA:ARBA00006219, ECO:0000256|PIRNR:PIRNR000706}.
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DR EMBL; CP000033; AAV43175.1; -; Genomic_DNA.
DR RefSeq; WP_003547977.1; NC_006814.3.
DR RefSeq; YP_194206.1; NC_006814.3.
DR AlphaFoldDB; Q5FJE9; -.
DR SMR; Q5FJE9; -.
DR STRING; 272621.LBA1348; -.
DR GeneID; 56942929; -.
DR KEGG; lac:LBA1348; -.
DR PATRIC; fig|272621.13.peg.1276; -.
DR eggNOG; COG3231; Bacteria.
DR HOGENOM; CLU_073027_1_0_9; -.
DR OrthoDB; 3806873at2; -.
DR BioCyc; LACI272621:G1G49-1325-MONOMER; -.
DR Proteomes; UP000006381; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008910; F:kanamycin kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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, ECO:0000313|EMBL:AAV43175.1};
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:UP000006381};
KW Transferase {ECO:0000256|PIRNR:PIRNR000706, ECO:0000313|EMBL:AAV43175.1}.
FT DOMAIN 34..243
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
FT ACT_SITE 185
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000706-1"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000706-2"
FT BINDING 203
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000706-2"
SQ SEQUENCE 260 AA; 29822 MW; 04F7AA061224BC0E CRC64;
MQKTILTKVP ENIPLDIYRF ISGAKIYDSS SSPEARVYFI DKDNGYYLKR SAIGKLEKEA
QMTEYFYSKG LSAEVLNYLS NDYDWLLTAA VGGEDCVYPK YLKNPERLCD TIACELRKLH
ETDYTDCPVM DKTINYLATA EKNYHTGNYD QSQFPSFGYS SAKEAYDILM SGKNALRDKV
LLHGDYCLPN IILKNWNFSG FIDVGGSGVG DRHIDLFWGA WTLWFNLKTN KYRNRFFDAY
GRDKVDESVL EVIAAAEVFE
//
