ID   S9AD_ENTFL              Reviewed;         255 AA.
AC   Q07448;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Spectinomycin 9-adenylyltransferase {ECO:0000303|PubMed:1659306};
DE   AltName: Full=AAD(9) {ECO:0000303|PubMed:1659306};
GN   Name=spc {ECO:0000303|PubMed:1659306};
GN   Synonyms=aad9 {ECO:0000303|PubMed:1659306};
OS   Enterococcus faecalis (Streptococcus faecalis).
OG   Plasmid pDL55.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1351;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN SPECTINOMYCIN RESISTANCE,
RP   AND CATALYTIC ACTIVITY.
RC   STRAIN=LDR55;
RX   PubMed=1659306; DOI=10.1128/aac.35.9.1804;
RA   Leblanc D.J., Lee L.N., Inamine J.M.;
RT   "Cloning and nucleotide base sequence analysis of a spectinomycin
RT   adenyltransferase AAD(9) determinant from Enterococcus faecalis.";
RL   Antimicrob. Agents Chemother. 35:1804-1810(1991).
CC   -!- FUNCTION: Mediates bacterial resistance to the antibiotic spectinomycin
CC       but not streptomycin. {ECO:0000269|PubMed:1659306}.
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:0000269|PubMed:1659306};
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DR   EMBL; M69221; AAA16527.1; -; Unassigned_DNA.
DR   PIR; A61153; A61153.
DR   RefSeq; WP_063840673.1; NG_047398.1.
DR   PDB; 6SXJ; X-ray; 2.10 A; A=1-255.
DR   PDB; 6XXQ; X-ray; 3.00 A; A/B=1-255.
DR   PDB; 6XZ0; X-ray; 2.80 A; A=1-255.
DR   PDBsum; 6SXJ; -.
DR   PDBsum; 6XXQ; -.
DR   PDBsum; 6XZ0; -.
DR   AlphaFoldDB; Q07448; -.
DR   SMR; Q07448; -.
DR   KEGG; ag:AAA16527; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IDA:UniProtKB.
DR   Gene3D; 3.30.460.10; -; 1.
DR   InterPro; IPR025184; DUF4111.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR041633; Polbeta.
DR   Pfam; PF13427; DUF4111; 1.
DR   Pfam; PF18765; Polbeta; 1.
DR   SUPFAM; SSF81301; SSF81301; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic resistance; ATP-binding; Nucleotide-binding;
KW   Nucleotidyltransferase; Plasmid; Transferase.
FT   CHAIN           1..255
FT                   /note="Spectinomycin 9-adenylyltransferase"
FT                   /id="PRO_0000068582"
FT   HELIX           8..23
FT                   /evidence="ECO:0007829|PDB:6SXJ"
FT   HELIX           24..26
FT                   /evidence="ECO:0007829|PDB:6SXJ"
FT   STRAND          27..34
FT                   /evidence="ECO:0007829|PDB:6SXJ"
FT   HELIX           35..38
FT                   /evidence="ECO:0007829|PDB:6SXJ"
FT   STRAND          47..55
FT                   /evidence="ECO:0007829|PDB:6SXJ"
FT   HELIX           59..69
FT                   /evidence="ECO:0007829|PDB:6SXJ"
FT   HELIX           70..72
FT                   /evidence="ECO:0007829|PDB:6SXJ"
FT   STRAND          85..92
FT                   /evidence="ECO:0007829|PDB:6SXJ"
FT   HELIX           93..95
FT                   /evidence="ECO:0007829|PDB:6SXJ"
FT   STRAND          106..108
FT                   /evidence="ECO:0007829|PDB:6SXJ"
FT   HELIX           110..112
FT                   /evidence="ECO:0007829|PDB:6SXJ"
FT   HELIX           113..117
FT                   /evidence="ECO:0007829|PDB:6SXJ"
FT   STRAND          124..126
FT                   /evidence="ECO:0007829|PDB:6XZ0"
FT   HELIX           130..139
FT                   /evidence="ECO:0007829|PDB:6SXJ"
FT   STRAND          142..148
FT                   /evidence="ECO:0007829|PDB:6SXJ"
FT   HELIX           150..153
FT                   /evidence="ECO:0007829|PDB:6SXJ"
FT   HELIX           159..173
FT                   /evidence="ECO:0007829|PDB:6SXJ"
FT   TURN            174..176
FT                   /evidence="ECO:0007829|PDB:6XZ0"
FT   HELIX           181..196
FT                   /evidence="ECO:0007829|PDB:6SXJ"
FT   HELIX           203..212
FT                   /evidence="ECO:0007829|PDB:6SXJ"
FT   HELIX           216..229
FT                   /evidence="ECO:0007829|PDB:6SXJ"
FT   HELIX           236..238
FT                   /evidence="ECO:0007829|PDB:6SXJ"
FT   HELIX           241..253
FT                   /evidence="ECO:0007829|PDB:6SXJ"
SQ   SEQUENCE   255 AA;  29821 MW;  367505B0CA0E68B4 CRC64;
     MRRIYLNTYE QINKVKKILR KHLKNNLIGT YMFGSGVESG LKPNSDLDFL VVVSEPLTDQ
     SKEILIQKIR PISKKIGDKS NLRYIELTII IQQEMVPWNH PPKQEFIYGE WLQELYEQGY
     IPQKELNSDL TIMLYQAKRK NKRIYGNYDL EELLPDIPFS DVRRAIMDSS EELIDNYQDD
     ETNSILTLCR MILTMDTGKI IPKDIAGNAV AESSPLEHRE RILLAVRSYL GENIEWTNEN
     VNLTINYLNN RLKKL