VGB_BORPA
ID VGB_BORPA Reviewed; 299 AA.
AC Q7WCA6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 89.
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}; OrderedLocusNames=BPP0421;
OS Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257311;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
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).
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; BX640424; CAE36005.1; -; Genomic_DNA.
DR RefSeq; WP_010927464.1; NC_002928.3.
DR AlphaFoldDB; Q7WCA6; -.
DR SMR; Q7WCA6; -.
DR EnsemblBacteria; CAE36005; CAE36005; BPP0421.
DR KEGG; bpa:BPP0421; -.
DR HOGENOM; CLU_054751_1_0_4; -.
DR OMA; ALWFTEW; -.
DR Proteomes; UP000001421; 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..299
FT /note="Virginiamycin B lyase"
FT /id="PRO_0000313769"
FT ACT_SITE 271
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01282"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01282"
FT BINDING 269
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01282"
FT BINDING 286
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01282"
SQ SEQUENCE 299 AA; 31193 MW; FF39A32F9D8EA525 CRC64;
MNQVEMTEFP VGKPQEALYG VASTPDGALW FTLAKGNAIG RLSPDGAVSR FPLPHTDGQP
TTITCGPDGR PWFTLSSANA IGRLAPDGAL RMFELPRPAS RPFGIAGGHD GCLWFAEMAG
DRIGRITIDG DIEEYDLPVK GGYPSCMAAG RDGLMWFTLN QAGAVGSISA TAAPRIFPLG
AADAAPVGIA SDAQGALWIA QAGNGAIVRF DAGGRITEFP LHSRAARPHA IAADAAGNLW
FTEWGANRIG RISEAGDLAG YELAAPGSEP HGIAIDPHGC VWAALETGRL VRLQASPRD