ID   FOSB_STAHA              Reviewed;         139 AA.
AC   Q55317;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 70.
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};
OS   Staphylococcus haemolyticus.
OG   Plasmid.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1993;
RX   PubMed=9338493; DOI=10.1093/jac/40.3.393;
RA   Arca P., Reguera G., Hardisson C.;
RT   "Plasmid-encoded fosfomycin resistance in bacteria isolated from the
RT   urinary tract in a multicentre survey.";
RL   J. Antimicrob. Chemother. 40:393-399(1997).
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; X89875; CAA61967.1; -; Genomic_DNA.
DR   PIR; S58181; S58181.
DR   RefSeq; WP_011276918.1; NZ_CUFU01000075.1.
DR   AlphaFoldDB; Q55317; -.
DR   SMR; Q55317; -.
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; Plasmid;
KW   Transferase.
FT   CHAIN           1..139
FT                   /note="Metallothiol transferase FosB"
FT                   /id="PRO_0000164041"
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   139 AA;  16394 MW;  39F2AF02B12ADA30 CRC64;
     MIKGINHITY SVSNIAKSIE FYRDILGADI LVESETSAYF NLGGIWLALN EEKNIPRSEI
     KYSYTHIAFT ISDNDFEDWY NWLKENEVNI LEGRDRDIRD KKSIYFTDLD GHKLELHTGS
     LEDRLSYYKE AKPHMNFYI