ID   AACA_STAEQ              Reviewed;         479 AA.
AC   Q5HMP3;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=SERP1585;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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; CP000029; AAW54933.1; -; Genomic_DNA.
DR   RefSeq; WP_001028144.1; NC_002976.3.
DR   AlphaFoldDB; Q5HMP3; -.
DR   SMR; Q5HMP3; -.
DR   STRING; 176279.SERP1585; -.
DR   EnsemblBacteria; AAW54933; AAW54933; SERP1585.
DR   GeneID; 58049990; -.
DR   GeneID; 61913521; -.
DR   GeneID; 66882989; -.
DR   KEGG; ser:SERP1585; -.
DR   eggNOG; COG1670; Bacteria.
DR   eggNOG; COG3173; Bacteria.
DR   HOGENOM; CLU_632450_0_0_9; -.
DR   OMA; IYKRTYR; -.
DR   OrthoDB; 164889at2; -.
DR   Proteomes; UP000000531; Chromosome.
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; Reference proteome;
KW   Transferase.
FT   CHAIN           1..479
FT                   /note="Bifunctional AAC/APH"
FT                   /id="PRO_0000223382"
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