ID   AACA_STAAM              Reviewed;         479 AA.
AC   P0A0C0; P14507;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Bifunctional AAC/APH;
DE   Includes:
DE     RecName: Full=6'-aminoglycoside N-acetyltransferase;
DE              EC=2.3.1.-;
DE     AltName: Full=AAC(6');
DE   Includes:
DE     RecName: Full=Aminoglycoside 2''-phosphotransferase;
DE     AltName: Full=2''-aminoglycoside phosphotransferase;
DE              EC=2.7.1.190 {ECO:0000250|UniProtKB:P0A0C2};
DE     AltName: Full=APH(2'');
GN   Name=aacA-aphD; OrderedLocusNames=SAVP026;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OG   Plasmid VRSAp.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699; PLASMID=VRSAp;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
CC   -!- FUNCTION: Involved in resistance to gentamicin, tobramycin, and
CC       kanamycin. Tobramycin and kanamycin resistance is due to the ACC
CC       activity, specified by N-terminal region. The C-terminal region is a
CC       kinase that phosphorylates several 4,6-disubstituted aminoglycosides.
CC       {ECO:0000250|UniProtKB:P0A0C2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a gentamycin + GTP = a gentamycin 2''-phosphate + GDP + H(+);
CC         Xref=Rhea:RHEA:48872, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:58189, ChEBI:CHEBI:90218, ChEBI:CHEBI:90219;
CC         EC=2.7.1.190; Evidence={ECO:0000250|UniProtKB:P0A0C2};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the aminoglycoside
CC       phosphotransferase family. {ECO:0000305}.
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DR   EMBL; AP003367; BAB47534.1; -; Genomic_DNA.
DR   RefSeq; WP_001028144.1; NC_002774.1.
DR   AlphaFoldDB; P0A0C0; -.
DR   SMR; P0A0C0; -.
DR   World-2DPAGE; 0002:P0A0C0; -.
DR   PaxDb; P0A0C0; -.
DR   EnsemblBacteria; BAB47534; BAB47534; BAB47534.
DR   GeneID; 58049990; -.
DR   GeneID; 61913521; -.
DR   GeneID; 66882989; -.
DR   KEGG; sav:SAVP026; -.
DR   HOGENOM; CLU_632450_0_0_9; -.
DR   OMA; IYKRTYR; -.
DR   BioCyc; SAUR158878:SAV_RS00105-MON; -.
DR   Proteomes; UP000002481; Plasmid VRSAp.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0034071; F:aminoglycoside phosphotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR002575; Aminoglycoside_PTrfase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   Pfam; PF01636; APH; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Antibiotic resistance; ATP-binding; Cytoplasm; Kinase;
KW   Multifunctional enzyme; Nucleotide-binding; Plasmid; Transferase.
FT   CHAIN           1..479
FT                   /note="Bifunctional AAC/APH"
FT                   /id="PRO_0000204797"
FT   DOMAIN          8..180
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          110..153
FT                   /note="Acetyl-CoA binding site"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        374
FT                   /note="Proton acceptor; for phosphotransferase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         393
FT                   /ligand="a gentamycin"
FT                   /ligand_id="ChEBI:CHEBI:90218"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   479 AA;  56855 MW;  744D93D76299CFCE CRC64;
     MNIVENEICI RTLIDDDFPL MLKWLTDERV LEFYGGRDKK YTLESLKKHY TEPWEDEVFR
     VIIEYNNVPI GYGQIYKMYD ELYTDYHYPK TDEIVYGMDQ FIGEPNYWSK GIGTRYIKLI
     FEFLKKERNA NAVILDPHKN NPRAIRAYQK SGFRIIEDLP EHELHEGKKE DCYLMEYRYD
     DNATNVKAMK YLIEHYFDNF KVDSIEIIGS GYDSVAYLVN NEYIFKTKFS TNKKKGYAKE
     KAIYNFLNTN LETNVKIPNI EYSYISDELS ILGYKEIKGT FLTPEIYSTM SEEEQNLLKR
     DIASFLRQMH GLDYTDISEC TIDNKQNVLE EYILLRETIY NDLTDIEKDY IESFMERLNA
     TTVFEGKKCL CHNDFSCNHL LLDGNNRLTG IIDFGDSGII DEYCDFIYLL EDSEEEIGTN
     FGEDILRMYG NIDIEKAKEY QDIVEEYYPI ETIVYGIKNI KQEFIENGRK EIYKRTYKD