ID AACA_STAAU Reviewed; 479 AA.
AC P0A0C1; P14507; Q7DG31;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 28-JUN-2023, entry version 109.
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; ORFNames=R015, VRA0030;
OS Staphylococcus aureus.
OG Plasmid VRSAp, Plasmid pSK41, and Plasmid pLW043.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=VRSAp; TRANSPOSON=Tn4001;
RX PubMed=2833561; DOI=10.1099/00221287-133-11-3039;
RA Rouch D.A., Byrne M.E., Kong Y.C., Skurray R.A.;
RT "The aacA-aphD gentamicin and kanamycin resistance determinant of Tn4001
RT from Staphylococcus aureus: expression and nucleotide sequence analysis.";
RL J. Gen. Microbiol. 133:3039-3052(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=pSK41;
RX PubMed=9721269; DOI=10.1128/jb.180.17.4350-4359.1998;
RA Berg T., Firth N., Apisiridej S., Hettiaratchi A., Leelaporn A.,
RA Skurray R.A.;
RT "Complete nucleotide sequence of pSK41: evolution of staphylococcal
RT conjugative multiresistance plasmids.";
RL J. Bacteriol. 180:4350-4359(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MR108;
RX PubMed=12654286; DOI=10.1016/s1368-7646(03)00003-7;
RA Ito T., Okuma K., Ma X.X., Yuzawa H., Hiramatsu K.;
RT "Insights on antibiotic resistance of Staphylococcus aureus from its whole
RT genome: genomic island SCC.";
RL Drug Resist. Updat. 6:41-52(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14645850; DOI=10.1126/science.1090956;
RA Weigel L.M., Clewell D.B., Gill S.R., Clark N.C., McDougal L.K.,
RA Flannagan S.E., Kolonay J.F., Shetty J., Killgore G.E., Tenover F.C.;
RT "Genetic analysis of a high-level vancomycin-resistant isolate of
RT Staphylococcus aureus.";
RL Science 302:1569-1571(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=7-0;
RA Ishikawa J., Izuta T., Katsumata Y., Ishino K., Matsumoto H., Hotta K.;
RT "Aminoglycoside resistance gene in Staphylococcus aureus.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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.
CC -!- SIMILARITY: In the C-terminal section; belongs to the aminoglycoside
CC phosphotransferase family. {ECO:0000305}.
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DR EMBL; GU565967; AAA88548.1; -; Genomic_DNA.
DR EMBL; AF051917; AAC61972.1; -; Genomic_DNA.
DR EMBL; AB096217; BAC67573.1; -; Genomic_DNA.
DR EMBL; AE017171; AAQ17152.1; -; Genomic_DNA.
DR EMBL; AB246921; BAE75929.1; -; Genomic_DNA.
DR PIR; S26353; S26353.
DR RefSeq; NP_863643.1; NC_005024.1.
DR RefSeq; NP_878008.1; NC_005054.1.
DR RefSeq; WP_001028144.1; NZ_WWCF01000093.1.
DR RefSeq; YP_001715988.1; NC_010419.1.
DR RefSeq; YP_002790939.1; NC_012547.1.
DR RefSeq; YP_003813125.1; NC_014369.1.
DR RefSeq; YP_006937626.1; NC_013320.1.
DR RefSeq; YP_006937700.1; NC_013321.1.
DR RefSeq; YP_006938333.1; NC_013338.1.
DR RefSeq; YP_006938359.1; NC_013339.1.
DR RefSeq; YP_006938464.1; NC_013342.1.
DR RefSeq; YP_006938543.1; NC_013343.1.
DR RefSeq; YP_006938602.1; NC_013344.1.
DR RefSeq; YP_008709805.1; NC_022598.1.
DR PDB; 4ORK; X-ray; 2.30 A; A/B/C/D=175-479.
DR PDB; 5BYL; X-ray; 2.15 A; A/B/C/D=175-479.
DR PDB; 5IQA; X-ray; 2.15 A; A/B/C/D=175-479.
DR PDB; 5IQB; X-ray; 2.30 A; A/B/C/D=175-479.
DR PDB; 5IQC; X-ray; 2.30 A; A/B/C/D=175-479.
DR PDB; 5IQD; X-ray; 2.20 A; A/B/C/D=175-479.
DR PDB; 5IQE; X-ray; 2.50 A; A/B/C/D=175-479.
DR PDB; 5IQF; X-ray; 2.35 A; A/B/C/D=175-479.
DR PDB; 5IQG; X-ray; 2.50 A; A/B/C/D=175-479.
DR PDB; 5IQH; X-ray; 2.25 A; A/B/C/D=175-479.
DR PDB; 5IQI; X-ray; 2.15 A; A/B/C/D=175-479.
DR PDB; 6C5U; X-ray; 2.41 A; A/B/C/D=175-479.
DR PDB; 6CAV; X-ray; 2.60 A; A/B/C/D=175-479.
DR PDB; 6CEY; X-ray; 2.40 A; A/B/C/D=175-479.
DR PDB; 6CGD; X-ray; 2.20 A; A/B/C/D=175-479.
DR PDB; 6CGG; X-ray; 2.40 A; A/B/C/D=175-479.
DR PDB; 6CH4; X-ray; 2.30 A; A/B/C/D=175-479.
DR PDBsum; 4ORK; -.
DR PDBsum; 5BYL; -.
DR PDBsum; 5IQA; -.
DR PDBsum; 5IQB; -.
DR PDBsum; 5IQC; -.
DR PDBsum; 5IQD; -.
DR PDBsum; 5IQE; -.
DR PDBsum; 5IQF; -.
DR PDBsum; 5IQG; -.
DR PDBsum; 5IQH; -.
DR PDBsum; 5IQI; -.
DR PDBsum; 6C5U; -.
DR PDBsum; 6CAV; -.
DR PDBsum; 6CEY; -.
DR PDBsum; 6CGD; -.
DR PDBsum; 6CGG; -.
DR PDBsum; 6CH4; -.
DR AlphaFoldDB; P0A0C1; -.
DR SMR; P0A0C1; -.
DR GeneID; 72384517; -.
DR OMA; IYKRTYR; -.
DR BRENDA; 2.7.1.190; 3352.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0034071; F:aminoglycoside phosphotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP 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; cd05120; APH_ChoK_like; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.90.1200.10; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR31438; LYSINE N-ACYLTRANSFERASE C17G9.06C-RELATED; 1.
DR PANTHER; PTHR31438:SF1; LYSINE N-ACYLTRANSFERASE C17G9.06C-RELATED; 1.
DR Pfam; PF13523; Acetyltransf_8; 1.
DR Pfam; PF01636; APH; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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; Transposable element.
FT CHAIN 1..479
FT /note="Bifunctional AAC/APH"
FT /id="PRO_0000204798"
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 HELIX 184..196
FT /evidence="ECO:0007829|PDB:5BYL"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:5BYL"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:5BYL"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:5BYL"
FT STRAND 223..230
FT /evidence="ECO:0007829|PDB:5BYL"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:4ORK"
FT HELIX 236..250
FT /evidence="ECO:0007829|PDB:5BYL"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:5BYL"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:5BYL"
FT STRAND 267..275
FT /evidence="ECO:0007829|PDB:5BYL"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:5BYL"
FT HELIX 284..289
FT /evidence="ECO:0007829|PDB:5BYL"
FT HELIX 292..311
FT /evidence="ECO:0007829|PDB:5BYL"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:5BYL"
FT HELIX 324..337
FT /evidence="ECO:0007829|PDB:5BYL"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:5BYL"
FT HELIX 345..360
FT /evidence="ECO:0007829|PDB:5BYL"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:5BYL"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:5BYL"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:5BYL"
FT STRAND 388..391
FT /evidence="ECO:0007829|PDB:5BYL"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:5BYL"
FT HELIX 402..406
FT /evidence="ECO:0007829|PDB:5BYL"
FT TURN 407..410
FT /evidence="ECO:0007829|PDB:5BYL"
FT STRAND 413..416
FT /evidence="ECO:0007829|PDB:5BYL"
FT HELIX 419..429
FT /evidence="ECO:0007829|PDB:5BYL"
FT HELIX 434..458
FT /evidence="ECO:0007829|PDB:5BYL"
FT HELIX 462..477
FT /evidence="ECO:0007829|PDB:5BYL"
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
//
