ID   FOSB_BACAH              Reviewed;         138 AA.
AC   A0RD31;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Metallothiol transferase FosB {ECO:0000255|HAMAP-Rule:MF_01512};
DE            EC=2.5.1.- {ECO:0000255|HAMAP-Rule:MF_01512};
DE   AltName: Full=Fosfomycin resistance protein {ECO:0000255|HAMAP-Rule:MF_01512};
GN   Name=fosB {ECO:0000255|HAMAP-Rule:MF_01512}; OrderedLocusNames=BALH_1802;
OS   Bacillus thuringiensis (strain Al Hakam).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=412694;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Al Hakam;
RX   PubMed=17337577; DOI=10.1128/jb.00241-07;
RA   Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D.,
RA   Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Green L.D., Han C.S., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA   Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D.,
RA   McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA   Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA   Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N.,
RA   Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S.;
RT   "The complete genome sequence of Bacillus thuringiensis Al Hakam.";
RL   J. Bacteriol. 189:3680-3681(2007).
CC   -!- FUNCTION: Metallothiol transferase which confers resistance to
CC       fosfomycin by catalyzing the addition of a thiol cofactor to
CC       fosfomycin. L-cysteine is probably the physiological thiol donor.
CC       {ECO:0000255|HAMAP-Rule:MF_01512}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01512};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01512}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01512}.
CC   -!- SIMILARITY: Belongs to the fosfomycin resistance protein family. FosB
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01512}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000485; ABK85124.1; -; Genomic_DNA.
DR   RefSeq; WP_000911694.1; NC_008600.1.
DR   AlphaFoldDB; A0RD31; -.
DR   SMR; A0RD31; -.
DR   EnsemblBacteria; ABK85124; ABK85124; BALH_1802.
DR   KEGG; btl:BALH_1802; -.
DR   HOGENOM; CLU_121356_0_0_9; -.
DR   OMA; ELWLCLS; -.
DR   Proteomes; UP000000761; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:UniProtKB-UniRule.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.180.10; -; 1.
DR   HAMAP; MF_01512; FosB; 1.
DR   InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR   InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR   InterPro; IPR022858; Metallothiol_Trafse_FosB.
DR   InterPro; IPR037523; VOC.
DR   Pfam; PF00903; Glyoxalase; 1.
DR   SUPFAM; SSF54593; SSF54593; 1.
DR   PROSITE; PS51819; VOC; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Cytoplasm; Magnesium; Metal-binding; Transferase.
FT   CHAIN           1..138
FT                   /note="Metallothiol transferase FosB"
FT                   /id="PRO_0000296657"
FT   DOMAIN          4..119
FT                   /note="VOC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   ACT_SITE        115
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   BINDING         7
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01512"
FT   BINDING         66
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01512"
FT   BINDING         115
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01512"
SQ   SEQUENCE   138 AA;  16524 MW;  F78857E3E778C0F1 CRC64;
     MLKGINHLCF SVSNLEDSIT FYEKVLEGEL LVRGRKLAYF NICGVWIALN EEIHIPRNEI
     HQSYTHIAFS VEQKDFERLL QRLEENDVHI LQGRERDVRD CESIYFVDPD GHKFEFHSGT
     LQERLNYYRE DKPHMTFY