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Database: UniProt
Entry: A3CPV7_STRSV
LinkDB: A3CPV7_STRSV
Original site: A3CPV7_STRSV 
ID   A3CPV7_STRSV            Unreviewed;       258 AA.
AC   A3CPV7;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=Aminoglycoside phosphotransferase, putative {ECO:0000313|EMBL:ABN45212.1};
DE            EC=2.7.1.95 {ECO:0000313|EMBL:ABN45212.1};
GN   OrderedLocusNames=SSA_1830 {ECO:0000313|EMBL:ABN45212.1};
OS   Streptococcus sanguinis (strain SK36).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=388919 {ECO:0000313|EMBL:ABN45212.1, ECO:0000313|Proteomes:UP000002148};
RN   [1] {ECO:0000313|EMBL:ABN45212.1, ECO:0000313|Proteomes:UP000002148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK36 {ECO:0000313|EMBL:ABN45212.1,
RC   ECO:0000313|Proteomes:UP000002148};
RX   PubMed=17277061; DOI=10.1128/JB.01808-06;
RA   Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA   Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA   Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT   "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL   J. Bacteriol. 189:3166-3175(2007).
CC   -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC       {ECO:0000256|ARBA:ARBA00006219, ECO:0000256|PIRNR:PIRNR000706}.
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DR   EMBL; CP000387; ABN45212.1; -; Genomic_DNA.
DR   RefSeq; WP_011837397.1; NC_009009.1.
DR   RefSeq; YP_001035762.1; NC_009009.1.
DR   AlphaFoldDB; A3CPV7; -.
DR   STRING; 388919.SSA_1830; -.
DR   KEGG; ssa:SSA_1830; -.
DR   PATRIC; fig|388919.9.peg.1736; -.
DR   eggNOG; COG3231; Bacteria.
DR   HOGENOM; CLU_073027_1_0_9; -.
DR   OrthoDB; 3806873at2; -.
DR   Proteomes; UP000002148; 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};
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:UP000002148};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000706, ECO:0000313|EMBL:ABN45212.1}.
FT   DOMAIN          37..249
FT                   /note="Aminoglycoside phosphotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF01636"
FT   ACT_SITE        182
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000706-1"
FT   BINDING         187
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000706-2"
FT   BINDING         201
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000706-2"
SQ   SEQUENCE   258 AA;  29581 MW;  D78FED83D98B7921 CRC64;
     MKAEKISLSL AQFPEQIRTY LEGANFYDSS SHSAASVFYT DTGYYLKIDQ KDQLAQEATL
     AKWFEEQGLG VPVVHYLTAD KDYLLTKEAE GKDALAFLQQ PEELCQTMAA ALRKLHSLQP
     QHFPIQHRLQ HYKEQAEENY QKGCFYQKAL LPQFHIQSRE EAYQLIQEQG HLLTADALIH
     GDAFLSNFIL KDAATFSCFI DVGLAGLSNR HIDLYWAIWS LTYNLSDPQY AELFLDYYGR
     KDVDTDKLRL IAAFEAFG
//
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