ID   STA_ECOLX               Reviewed;         174 AA.
AC   P13018;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Streptothricin acetyltransferase {ECO:0000250|UniProtKB:P37506};
DE            EC=2.3.-.- {ECO:0000250|UniProtKB:P37506};
GN   Name=sat-1;
GN   and
GN   Name=sat-2;
OS   Escherichia coli.
OG   Plasmid R483.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IE 956 0180:H-; TRANSPOSON=Tn1825;
RX   PubMed=2550905; DOI=10.1093/nar/17.17.7103;
RA   Heim U., Tietze E., Weschke W., Tschaepe H., Wobus U.;
RT   "Nucleotide sequence of a plasmid born streptothricin-acetyl-transferase
RT   gene (sat-1).";
RL   Nucleic Acids Res. 17:7103-7103(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TRANSPOSON=Tn1826;
RX   PubMed=2157196; DOI=10.1093/nar/18.5.1283;
RA   Tietze E., Brevet J.;
RT   "Nucleotide sequence of the streptothricin-acetyl-transferase gene sat-2.";
RL   Nucleic Acids Res. 18:1283-1283(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   PLASMID=R483; TRANSPOSON=Tn7;
RX   PubMed=1850404; DOI=10.1128/jb.173.9.3025-3028.1991;
RA   Sundstroem L., Roy P.H., Skoeld O.;
RT   "Site-specific insertion of three structural gene cassettes in transposon
RT   Tn7.";
RL   J. Bacteriol. 173:3025-3028(1991).
CC   -!- FUNCTION: Involved in resistance to streptothricin, a broad-spectrum
CC       antibiotic produced by streptomycetes (PubMed:1850404). Detoxifies
CC       streptothricin via acetylation of the beta amino group of the first
CC       beta-lysyl moiety of streptothricin (By similarity).
CC       {ECO:0000250|UniProtKB:P37506, ECO:0000269|PubMed:1850404}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + streptothricin F = CoA + H(+) + N(beta)-
CC         acetylstreptothricin F; Xref=Rhea:RHEA:57000, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:60822,
CC         ChEBI:CHEBI:141394; Evidence={ECO:0000250|UniProtKB:P37506};
CC   -!- MISCELLANEOUS: Encoded in several related transposons, in
CC       (PubMed:2550905) encoded on an unnamed plasmid.
CC       {ECO:0000269|PubMed:1850404, ECO:0000269|PubMed:2550905}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. GNAT subfamily.
CC       {ECO:0000305}.
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DR   EMBL; X15995; CAA34124.1; -; Genomic_DNA.
DR   EMBL; X51546; CAA35921.1; -; Genomic_DNA.
DR   EMBL; M63169; AAA27469.1; -; Genomic_DNA.
DR   PIR; S05574; S05574.
DR   RefSeq; NP_065310.1; NC_002525.1.
DR   RefSeq; WP_000704156.1; NZ_WWEV01000054.1.
DR   RefSeq; YP_004422907.1; NC_015472.1.
DR   AlphaFoldDB; P13018; -.
DR   SMR; P13018; -.
DR   GeneID; 58164745; -.
DR   KEGG; ag:CAA35921; -.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR008125; Streptothricin_AcTrfase.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   PRINTS; PR01754; SACTRNSFRASE.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Antibiotic resistance; Plasmid; Transferase.
FT   CHAIN           1..174
FT                   /note="Streptothricin acetyltransferase"
FT                   /id="PRO_0000068588"
FT   DOMAIN          20..170
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ   SEQUENCE   174 AA;  19671 MW;  AE3290B03E646009 CRC64;
     MKISVIPEQV AETLDAENHF IVREVFDVHL SDQGFELSTR SVSPYRKDYI SDDDSDEDSA
     CYGAFIDQEL VGKIELNSTW NDLASIEHIV VSHTHRGKGV AHSLIEFAKK WALSRQLLGI
     RLETQTNNVP ACNLYAKCGF TLGGIDLFTY KTRPQVSNET AMYWYWFSGA QDDA