VATD_ENTFC
ID VATD_ENTFC Reviewed; 209 AA.
AC P50870;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Streptogramin A acetyltransferase;
DE EC=2.3.1.-;
DE AltName: Full=Virginiamycin acetyltransferase D;
DE Short=Vat(D);
GN Name=vatD; Synonyms=satA;
OS Enterococcus faecium (Streptococcus faecium).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1352;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BM4145;
RX PubMed=8257133; DOI=10.1128/aac.37.10.2119;
RA Rende-Fournier R., Leclercq R., Galimand M., Duval J., Courvalin P.;
RT "Identification of the satA gene encoding a streptogramin A
RT acetyltransferase in Enterococcus faecium BM4145.";
RL Antimicrob. Agents Chemother. 37:2119-2125(1993).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=11841212; DOI=10.1021/bi011991b;
RA Sugantino M., Roderick S.L.;
RT "Crystal structure of Vat(D): an acetyltransferase that inactivates
RT streptogramin group A antibiotics.";
RL Biochemistry 41:2209-2216(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND MUTAGENESIS OF HIS-82.
RX PubMed=12771141; DOI=10.1074/jbc.m303766200;
RA Kehoe L.E., Snidwongse J., Courvalin P., Rafferty J.B., Murray I.A.;
RT "Structural basis of Synercid (quinupristin-dalfopristin) resistance in
RT Gram-positive bacterial pathogens.";
RL J. Biol. Chem. 278:29963-29970(2003).
CC -!- FUNCTION: Inactivates the A compounds of streptogramin antibiotics by
CC acetylation, thus providing resistance to these antibiotics.
CC -!- SUBUNIT: Homohexamer.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000305}.
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DR EMBL; L12033; AAA24783.1; -; Genomic_DNA.
DR RefSeq; WP_002295712.1; NZ_PTVH01000201.1.
DR PDB; 1KHR; X-ray; 2.80 A; A/B/C/D/E/F=1-209.
DR PDB; 1KK4; X-ray; 2.70 A; A/B/C/D/E/F=1-209.
DR PDB; 1KK5; X-ray; 2.70 A; A/B/C/D/E/F=1-209.
DR PDB; 1KK6; X-ray; 2.50 A; A/B/C=1-209.
DR PDB; 1MR7; X-ray; 1.80 A; A/B/C/X/Y/Z=1-209.
DR PDB; 1MR9; X-ray; 3.00 A; A/B/C/X/Y/Z=1-209.
DR PDB; 1MRL; X-ray; 2.80 A; A/B/C=1-209.
DR PDB; 3DHO; X-ray; 1.80 A; A/B/C/D/E/F=1-209.
DR PDBsum; 1KHR; -.
DR PDBsum; 1KK4; -.
DR PDBsum; 1KK5; -.
DR PDBsum; 1KK6; -.
DR PDBsum; 1MR7; -.
DR PDBsum; 1MR9; -.
DR PDBsum; 1MRL; -.
DR PDBsum; 3DHO; -.
DR AlphaFoldDB; P50870; -.
DR SMR; P50870; -.
DR DrugBank; DB01992; Coenzyme A.
DR DrugBank; DB01764; Dalfopristin.
DR DrugBank; DB01669; Virginiamycin M1.
DR KEGG; ag:AAA24783; -.
DR EvolutionaryTrace; P50870; -.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR Pfam; PF00132; Hexapep; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Antibiotic resistance; Repeat; Transferase.
FT CHAIN 1..209
FT /note="Streptogramin A acetyltransferase"
FT /id="PRO_0000068663"
FT ACT_SITE 82
FT MUTAGEN 82
FT /note="H->A: 105-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:12771141"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:1KK4"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:1MR7"
FT HELIX 20..24
FT /evidence="ECO:0007829|PDB:1MR7"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:1MR7"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:1MR7"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:1MR7"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:1MR7"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1MR7"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:1MR7"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1MR7"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:1MR7"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:1MR7"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:1MR7"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:1MR7"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:1MR7"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:1MR7"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:1MR7"
FT TURN 158..161
FT /evidence="ECO:0007829|PDB:1MR7"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:1MR7"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:1MR7"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:1MR7"
FT HELIX 186..191
FT /evidence="ECO:0007829|PDB:1MR7"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:1MR7"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:1MR7"
SQ SEQUENCE 209 AA; 23649 MW; 75F52F1DD0C135C1 CRC64;
MGPNPMKMYP IEGNKSVQFI KPILEKLENV EVGEYSYYDS KNGETFDKQI LYHYPILNDK
LKIGKFCSIG PGVTIIMNGA NHRMDGSTYP FNLFGNGWEK HMPKLDQLPI KGDTIIGNDV
WIGKDVVIMP GVKIGDGAIV AANSVVVKDI APYMLAGGNP ANEIKQRFDQ DTINQLLDIK
WWNWPIDIIN ENIDKILDNS IIREVIWKK
