ID   FOSB_BACHK              Reviewed;         138 AA.
AC   Q6HJT7;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=BT9727_1857;
OS   Bacillus thuringiensis subsp. konkukian (strain 97-27).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=281309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=97-27;
RX   PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., 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   Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA   Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA   Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA   Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA   Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
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}.
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DR   EMBL; AE017355; AAT59669.1; -; Genomic_DNA.
DR   RefSeq; WP_000911687.1; NC_005957.1.
DR   RefSeq; YP_036189.1; NC_005957.1.
DR   AlphaFoldDB; Q6HJT7; -.
DR   SMR; Q6HJT7; -.
DR   EnsemblBacteria; AAT59669; AAT59669; BT9727_1857.
DR   KEGG; btk:BT9727_1857; -.
DR   PATRIC; fig|281309.8.peg.1956; -.
DR   HOGENOM; CLU_121356_0_0_9; -.
DR   OMA; ELWLCLS; -.
DR   Proteomes; UP000001301; 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_0000164029"
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;  16462 MW;  766F168028443320 CRC64;
     MLKGINHLCF SVSNLEDSIT FYEKVLEGEL LVKGRKLAYF NICGVWIALN EEIHIPRNEI
     HQSYTHIAFS VEQKDFERLL QRLEENDVHI LQGRERDVRD CESIYIVDPD GHKFEFHSGT
     LQERLNYYRE DKPHMTFY