ID   FOSB_BACCR              Reviewed;         138 AA.
AC   Q81EF2;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=BC_2027;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
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; AE016877; AAP08996.1; -; Genomic_DNA.
DR   RefSeq; NP_831795.1; NC_004722.1.
DR   RefSeq; WP_000943772.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q81EF2; -.
DR   SMR; Q81EF2; -.
DR   STRING; 226900.BC_2027; -.
DR   EnsemblBacteria; AAP08996; AAP08996; BC_2027.
DR   KEGG; bce:BC2027; -.
DR   PATRIC; fig|226900.8.peg.2036; -.
DR   HOGENOM; CLU_121356_0_0_9; -.
DR   OMA; ELWLCLS; -.
DR   Proteomes; UP000001417; 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;
KW   Reference proteome; Transferase.
FT   CHAIN           1..138
FT                   /note="Metallothiol transferase FosB"
FT                   /id="PRO_0000164026"
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;  16460 MW;  10523B47DF04D8EC CRC64;
     MLRGINHICF SVSNLENSIM FYEKVLEGEL LVKGRKLAYF NICGVWIALN EETHIPRNEV
     HQSYTHIAFS VEQEDFKCLI QRLEENDVHI LQGRERDVRD CESIYFVDPD GHKFEFHSGT
     LQDRLNYYRD EKPHMTFY