ID   S3AD_RHIRD              Reviewed;         269 AA.
AC   P14511;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Aminoglycoside (3'') (9) adenylyltransferase;
DE            EC=2.7.7.47;
DE   AltName: Full=Streptomycin 3''-adenylyltransferase;
DE            Short=SP-R {ECO:0000303|PubMed:2998941};
OS   Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium
OS   radiobacter).
OG   Plasmid IncW pSa.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=358;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN SPECTINOMYCIN AND PROBABLE
RP   STREPTOMYCIN RESISTANCE, AND DISRUPTION PHENOTYPE.
RX   PubMed=2998941; DOI=10.1016/0378-1119(85)90073-3;
RA   Tait R.C., Rempel H., Rodriguez R.L., Kado C.I.;
RT   "The aminoglycoside-resistance operon of the plasmid pSa: nucleotide
RT   sequence of the streptomycin-spectinomycin resistance gene.";
RL   Gene 36:97-104(1985).
RN   [2]
RP   FUNCTION.
RX   PubMed=6287164; DOI=10.1007/bf00422905;
RA   Tait R.C., Lundquist R.C., Kado C.I.;
RT   "Genetic map of the crown gall suppressive IncW plasmid pSa.";
RL   Mol. Gen. Genet. 186:10-15(1982).
CC   -!- FUNCTION: Mediates bacterial resistance to the antibiotic spectinomycin
CC       and probably also to streptomycin. {ECO:0000269|PubMed:2998941,
CC       ECO:0000269|PubMed:6287164}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + streptomycin = 3''-O-adenylylstreptomycin + diphosphate;
CC         Xref=Rhea:RHEA:20245, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58007, ChEBI:CHEBI:58605; EC=2.7.7.47;
CC         Evidence={ECO:0000305|PubMed:2998941};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + spectinomycin = 9-O-adenylylspectinomycin + diphosphate;
CC         Xref=Rhea:RHEA:63228, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:146260, ChEBI:CHEBI:146261;
CC         Evidence={ECO:0000305|PubMed:2998941};
CC   -!- DISRUPTION PHENOTYPE: Loss of resistance to spectinomycin.
CC       {ECO:0000269|PubMed:2998941}.
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DR   EMBL; M11444; AAA25647.1; -; Genomic_DNA.
DR   AlphaFoldDB; P14511; -.
DR   SMR; P14511; -.
DR   GO; GO:0009012; F:aminoglycoside 3''-adenylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   InterPro; IPR025184; DUF4111.
DR   InterPro; IPR043519; NT_sf.
DR   Pfam; PF13427; DUF4111; 1.
DR   SUPFAM; SSF81301; SSF81301; 1.
PE   1: Evidence at protein level;
KW   Antibiotic resistance; ATP-binding; Nucleotide-binding;
KW   Nucleotidyltransferase; Plasmid; Transferase.
FT   CHAIN           1..269
FT                   /note="Aminoglycoside (3'') (9) adenylyltransferase"
FT                   /id="PRO_0000068583"
SQ   SEQUENCE   269 AA;  30157 MW;  3CAF758E8908DD44 CRC64;
     MSNVRHHEGS VTIEISNQLS EVLSVIERHS GINVAGRAFV RSAVDGGLKP YSDIDLLVTV
     AVKLDETTRR ALLNDLMEAS AFPGESETLR AIEVTLVVHD DIIPWRYPAK RELQFGEWQR
     NDILAGIFEP AMIDIDLAIL LTKAREHSVA LVGPAAEEFF DPVPEQDLFE ALRETLKLWN
     SQPDWAGDER NVVLTLSRIW YSAITGKIAP KDVAADWAIK RLPAQYQPVL LEAKQAYLGQ
     KEDHLASRAD HLEEFIRFVK GEIIKSVGK