ID   S9AD_STAAU              Reviewed;         260 AA.
AC   P0A0D2; P04827;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Spectinomycin 9-adenylyltransferase;
DE   AltName: Full=AAD(9);
GN   Name=ant; Synonyms=spc {ECO:0000303|PubMed:2993813};
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN SPECTINOMYCIN RESISTANCE,
RP   AND MUTAGENESIS OF ALA-165.
RC   STRAIN=NCTC 8325; TRANSPOSON=Tn554;
RX   PubMed=2993813; DOI=10.1007/bf00383309;
RA   Murphy E.;
RT   "Nucleotide sequence of a spectinomycin adenyltransferase AAD(9)
RT   determinant from Staphylococcus aureus and its relationship to AAD(3')
RT   (9).";
RL   Mol. Gen. Genet. 200:33-39(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NCTC 8325; TRANSPOSON=Tn554;
RX   PubMed=3004956; DOI=10.1002/j.1460-2075.1985.tb04089.x;
RA   Murphy E., Huwyler L., Do Carno de Freire Bastos M.;
RT   "Transposon Tn554: complete nucleotide sequence and isolation of
RT   transposition-defective and antibiotic-sensitive mutants.";
RL   EMBO J. 4:3357-3365(1985).
CC   -!- FUNCTION: Mediates bacterial resistance to the antibiotic spectinomycin
CC       but not streptomycin. {ECO:0000269|PubMed:2993813}.
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:2993813};
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DR   EMBL; X02588; CAA26428.1; -; Genomic_DNA.
DR   EMBL; X03216; CAA26963.1; -; Genomic_DNA.
DR   PIR; D24584; D24584.
DR   RefSeq; WP_000067268.1; NZ_WWCF01000004.1.
DR   AlphaFoldDB; P0A0D2; -.
DR   SMR; P0A0D2; -.
DR   GeneID; 42043718; -.
DR   GeneID; 58051002; -.
DR   KEGG; ag:CAA26428; -.
DR   OMA; VRPWRYP; -.
DR   GO; GO:0070566; F:adenylyltransferase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IMP:UniProtKB.
DR   Gene3D; 3.30.460.10; -; 1.
DR   InterPro; IPR024172; AadA/Aad9.
DR   InterPro; IPR025184; DUF4111.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR   Pfam; PF13427; DUF4111; 1.
DR   Pfam; PF01909; NTP_transf_2; 1.
DR   PIRSF; PIRSF000819; Streptomycin_3-adenylyltransf; 1.
DR   SUPFAM; SSF81301; SSF81301; 1.
PE   1: Evidence at protein level;
KW   Antibiotic resistance; ATP-binding; Nucleotide-binding;
KW   Nucleotidyltransferase; Transferase; Transposable element.
FT   CHAIN           1..260
FT                   /note="Spectinomycin 9-adenylyltransferase"
FT                   /id="PRO_0000068586"
FT   MUTAGEN         165
FT                   /note="A->T: Loss of spectinomycin resistance and of
FT                   spectinomycin adenylylase activity."
FT                   /evidence="ECO:0000269|PubMed:2993813"
SQ   SEQUENCE   260 AA;  28975 MW;  3C821F312A108F54 CRC64;
     MSNLINGKIP NQAIQTLKIV KDLFGSSIVG VYLFGSAVNG GLRINSDVDV LVVVNHSLPQ
     LTRKKLTERL MTISGKIGNT DSVRPLEVTV INRSEVVPWQ YPPKREFIYG EWLRGEFENG
     QIQEPSYDPD LAIVLAQARK NSISLFGPDS SSILVSVPLT DIRRAIKDSL PELIEGIKGD
     ERNVILTLAR MWQTVTTGEI TSKDVAAEWA IPLLPKEHVT LLDIARKGYR GECDDKWEGL
     YSKVKALVKY MKNSIETSLN