ID   VGB_BACMK               Reviewed;         296 AA.
AC   A9VQJ9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Virginiamycin B lyase {ECO:0000255|HAMAP-Rule:MF_01282};
DE            EC=4.2.99.- {ECO:0000255|HAMAP-Rule:MF_01282};
DE   AltName: Full=Streptogramin B lyase {ECO:0000255|HAMAP-Rule:MF_01282};
GN   Name=vgb {ECO:0000255|HAMAP-Rule:MF_01282};
GN   OrderedLocusNames=BcerKBAB4_1749;
OS   Bacillus mycoides (strain KBAB4) (Bacillus weihenstephanensis).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBAB4;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
CC   -!- FUNCTION: Inactivates the type B streptogramin antibiotics by
CC       linearizing the lactone ring at the ester linkage, generating a free
CC       phenylglycine carboxylate and converting the threonyl moiety into 2-
CC       amino-butenoic acid. {ECO:0000255|HAMAP-Rule:MF_01282}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01282};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01282}.
CC   -!- SIMILARITY: Belongs to the Vgb family. {ECO:0000255|HAMAP-
CC       Rule:MF_01282}.
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DR   EMBL; CP000903; ABY42984.1; -; Genomic_DNA.
DR   RefSeq; WP_001223216.1; NC_010184.1.
DR   AlphaFoldDB; A9VQJ9; -.
DR   SMR; A9VQJ9; -.
DR   STRING; 315730.BcerKBAB4_1749; -.
DR   EnsemblBacteria; ABY42984; ABY42984; BcerKBAB4_1749.
DR   KEGG; bwe:BcerKBAB4_1749; -.
DR   eggNOG; COG4257; Bacteria.
DR   HOGENOM; CLU_054751_1_0_9; -.
DR   OMA; ALWFTEW; -.
DR   Proteomes; UP000002154; Chromosome.
DR   GO; GO:0016835; F:carbon-oxygen lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0017001; P:antibiotic catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 1.
DR   HAMAP; MF_01282; VirginiamycinB_lyase; 1.
DR   InterPro; IPR011217; Streptogrm_lyase.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PIRSF; PIRSF026412; Streptogrm_lyase; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..296
FT                   /note="Virginiamycin B lyase"
FT                   /id="PRO_1000140357"
FT   ACT_SITE        270
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01282"
FT   BINDING         228
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01282"
FT   BINDING         268
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01282"
FT   BINDING         285
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01282"
SQ   SEQUENCE   296 AA;  32484 MW;  81900505F530F67E CRC64;
     MRITIQEYVV NEIDSGPYGI TVGKDGALWF TEQKGNRIGR INATGEINSF PIPTANAGAM
     SIISDQTGDL WFTEYNSSKI GKMSMNGLFE EYVLPTTNAA PFGITEGPDG AIWFTEMNNG
     RIGRITKSGE ITEFELPNSK SFPSFITLGS DGALWFTQNQ NNRIGRITTK GEVKEYPIPT
     PNSGPVGIAS GPDGAIWFVQ IIGNKIGRIT FEGEIKEFVI PTPNARPHAI IPGKNRDLWF
     TEWGGNQISR ITVEGVITEY TIPTNNAEPH GITFCPDGDL WFAEECNQIG RLTIIT