AACA_STAWA
ID AACA_STAWA Reviewed; 479 AA.
AC Q7ATH7; Q7WTC3;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 80.
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;
OS Staphylococcus warneri.
OG Plasmid pGTK1, and Plasmid pGTK3.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12716781; DOI=10.1093/jac/dkg257;
RA Lange C.C., Werckenthin C., Schwarz S.;
RT "Molecular analysis of the plasmid-borne aacA/aphD resistance gene region
RT of coagulase-negative staphylococci from chickens.";
RL J. Antimicrob. Chemother. 51:1397-1401(2003).
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; AJ536195; CAD60196.1; -; Genomic_DNA.
DR EMBL; AJ536196; CAD60199.1; -; Genomic_DNA.
DR RefSeq; WP_001028144.1; NZ_JPOW01000008.1.
DR RefSeq; WP_032490744.1; NG_047212.1.
DR PDB; 4QC6; X-ray; 1.30 A; A/B=1-179.
DR PDBsum; 4QC6; -.
DR AlphaFoldDB; Q7ATH7; -.
DR SMR; Q7ATH7; -.
DR GeneID; 58049990; -.
DR GeneID; 61913521; -.
DR GeneID; 66882989; -.
DR BRENDA; 2.3.1.82; 5885.
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 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Antibiotic resistance; ATP-binding;
KW Cytoplasm; Kinase; Multifunctional enzyme; Nucleotide-binding; Plasmid;
KW Transferase.
FT CHAIN 1..479
FT /note="Bifunctional AAC/APH"
FT /id="PRO_0000223385"
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"
FT VARIANT 182
FT /note="N -> I (in plasmid pGTK3)"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:4QC6"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:4QC6"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:4QC6"
FT HELIX 18..24
FT /evidence="ECO:0007829|PDB:4QC6"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:4QC6"
FT TURN 32..35
FT /evidence="ECO:0007829|PDB:4QC6"
FT HELIX 43..49
FT /evidence="ECO:0007829|PDB:4QC6"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:4QC6"
FT STRAND 68..77
FT /evidence="ECO:0007829|PDB:4QC6"
FT HELIX 80..86
FT /evidence="ECO:0007829|PDB:4QC6"
FT STRAND 95..103
FT /evidence="ECO:0007829|PDB:4QC6"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:4QC6"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:4QC6"
FT HELIX 112..128
FT /evidence="ECO:0007829|PDB:4QC6"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:4QC6"
FT HELIX 142..151
FT /evidence="ECO:0007829|PDB:4QC6"
FT STRAND 154..165
FT /evidence="ECO:0007829|PDB:4QC6"
FT STRAND 168..177
FT /evidence="ECO:0007829|PDB:4QC6"
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
