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AACA_STAAU
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   03-AUG-2022, entry version 104.
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; Firmicutes; 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; 58049990; -.
DR   GeneID; 61913521; -.
DR   GeneID; 66882989; -.
DR   OMA; IYKRTYR; -.
DR   BRENDA; 2.7.1.190; 3352.
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; 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
 
 
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