VATA_STAAU
ID VATA_STAAU Reviewed; 219 AA.
AC P26839;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Virginiamycin A acetyltransferase;
DE EC=2.3.1.-;
GN Name=vat;
OS Staphylococcus aureus.
OG Plasmid pIP630.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8344533; DOI=10.1016/0378-1119(93)90350-c;
RA Allignet J., Loncle V., Simenel C., Delpierre M., el Solh N.;
RT "Sequence of a staphylococcal gene, vat, encoding an acetyltransferase
RT inactivating the A-type compounds of virginiamycin-like antibiotics.";
RL Gene 130:91-98(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-112.
RX PubMed=3149758; DOI=10.1016/0147-619x(88)90034-0;
RA Allignet J., Loncle V., Mazodier P., El Solh N.;
RT "Nucleotide sequence of a staphylococcal plasmid gene, vgb, encoding a
RT hydrolase inactivating the B components of virginiamycin-like
RT antibiotics.";
RL Plasmid 20:271-275(1988).
CC -!- FUNCTION: Inactivates the A compounds of virginiamycin-like
CC antibiotics, thus providing resistance to these antibiotics.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000305}.
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DR EMBL; L07778; AAA26683.1; -; Genomic_DNA.
DR EMBL; M36022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; JN0822; JN0822.
DR RefSeq; WP_032489635.1; NG_048537.1.
DR PDB; 4HUR; X-ray; 2.15 A; A/B/C=1-219.
DR PDB; 4HUS; X-ray; 2.36 A; A/B/C=1-219.
DR PDB; 4MYO; X-ray; 2.70 A; A/B/C=7-219.
DR PDB; 6X3C; X-ray; 3.05 A; A/B/C/D/E/F=7-213.
DR PDB; 6X3J; X-ray; 2.70 A; A/B/C/D/E/F=7-215.
DR PDBsum; 4HUR; -.
DR PDBsum; 4HUS; -.
DR PDBsum; 4MYO; -.
DR PDBsum; 6X3C; -.
DR PDBsum; 6X3J; -.
DR AlphaFoldDB; P26839; -.
DR SMR; P26839; -.
DR KEGG; ag:AAA26683; -.
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; Plasmid; Repeat;
KW Transferase.
FT CHAIN 1..219
FT /note="Virginiamycin A acetyltransferase"
FT /id="PRO_0000068664"
FT ACT_SITE 87
FT /evidence="ECO:0000250"
FT CONFLICT 1
FT /note="M -> L (in Ref. 2)"
FT /evidence="ECO:0000305"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:4HUR"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:4HUR"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:4HUR"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:4HUR"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:4HUR"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:4HUR"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:4HUR"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:4HUR"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:4HUR"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:4HUR"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:4HUR"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:4HUR"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:4HUR"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:4HUR"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:4HUR"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:4HUR"
FT TURN 163..166
FT /evidence="ECO:0007829|PDB:4HUR"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:4HUR"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:4HUR"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:4HUR"
FT HELIX 191..203
FT /evidence="ECO:0007829|PDB:4HUR"
FT HELIX 206..215
FT /evidence="ECO:0007829|PDB:4HUR"
SQ SEQUENCE 219 AA; 24932 MW; CDAFD846D0727207 CRC64;
MNLNNDHGPD PENILPIKGN RNLQFIKPTI TNENILVGEY SYYDSKRGES FEDQVLYHYE
VIGDKLIIGR FCSIGPGTTF IMNGANHRMD GSTYPFHLFR MGWEKYMPSL KDLPLKGDIE
IGNDVWIGRD VTIMPGVKIG DGAIIAAEAV VTKNVAPYSI VGGNPLKFIR KRFSDGVIEE
WLALQWWNLD MKIINENLPF IINGDIEMLK RKRKLLDDT