ID   VGB_BORPE               Reviewed;         299 AA.
AC   Q7W0D3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Virginiamycin B lyase;
DE            EC=4.2.99.-;
DE   AltName: Full=Streptogramin B lyase;
GN   Name=vgb; OrderedLocusNames=BP0212;
OS   Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257313;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
RN   [2]
RP   FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=11467949; DOI=10.1021/bi0106787;
RA   Mukhtar T.A., Koteva K.P., Hughes D.W., Wright G.D.;
RT   "Vgb from Staphylococcus aureus inactivates streptogramin B antibiotics by
RT   an elimination mechanism not hydrolysis.";
RL   Biochemistry 40:8877-8886(2001).
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:0000269|PubMed:11467949}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=31 uM for quinupristin {ECO:0000269|PubMed:11467949};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Vgb family. {ECO:0000305}.
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DR   EMBL; BX640411; CAE40592.1; -; Genomic_DNA.
DR   RefSeq; NP_879100.1; NC_002929.2.
DR   RefSeq; WP_010929687.1; NZ_CP039022.1.
DR   AlphaFoldDB; Q7W0D3; -.
DR   SMR; Q7W0D3; -.
DR   STRING; 257313.BP0212; -.
DR   GeneID; 45387732; -.
DR   KEGG; bpe:BP0212; -.
DR   PATRIC; fig|257313.5.peg.229; -.
DR   eggNOG; COG4257; Bacteria.
DR   HOGENOM; CLU_054751_1_0_4; -.
DR   OMA; ALWFTEW; -.
DR   SABIO-RK; Q7W0D3; -.
DR   Proteomes; UP000002676; 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   1: Evidence at protein level;
KW   Antibiotic resistance; Lyase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..299
FT                   /note="Virginiamycin B lyase"
FT                   /id="PRO_0000313770"
FT   ACT_SITE        271
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         229
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         269
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         286
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   299 AA;  31143 MW;  0A2F6EB90ABDF822 CRC64;
     MNQVEMTEFP VGKPEEALYG VASTPDGALW FTLAKGNAIG RLSPDGEVSR FPLPHADGQP
     TTITCGPDGR PWFTLSSANA VGRLSPDGAL RMFELPRPAS RPFGIAAGHD GCLWFAEMAG
     DRIGRITIDG DIEEYDLPVK GGYPSCMAAG RDGLMWFTLN QAGAIGSISA TAAPRIFPLG
     AADAAPVGIA SDAQGALWIA QAGNGAIARF DAGGRITEFP LHSRAARPHA LAADAAGNLW
     FTEWGANRIG RISEAGDTAG YELAAPGSEP HGIAIDPHGC VWAALETGSL VRLQASPRD