ID   FOSB_BREBN              Reviewed;         141 AA.
AC   C0ZJ12;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=BBR47_44100;
OS   Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=358681;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=47 / JCM 6285 / NBRC 100599;
RA   Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W.,
RA   Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S.,
RA   Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H.,
RA   Udaka S., Tanikawa S., Fujita N.;
RT   "Brevibacillus brevis strain 47, complete genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; AP008955; BAH45387.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0ZJ12; -.
DR   SMR; C0ZJ12; -.
DR   STRING; 358681.BBR47_44100; -.
DR   EnsemblBacteria; BAH45387; BAH45387; BBR47_44100.
DR   KEGG; bbe:BBR47_44100; -.
DR   eggNOG; COG0346; Bacteria.
DR   HOGENOM; CLU_121356_0_0_9; -.
DR   OMA; IPRNDIQ; -.
DR   Proteomes; UP000001877; 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..141
FT                   /note="Metallothiol transferase FosB"
FT                   /id="PRO_0000383365"
FT   DOMAIN          6..121
FT                   /note="VOC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   ACT_SITE        117
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01512"
FT   BINDING         68
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01512"
FT   BINDING         117
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01512"
SQ   SEQUENCE   141 AA;  16874 MW;  427BD4FAA088FC96 CRC64;
     MPQLQGLNHL LFSVSDLEKS FCFYRDVLHA KPLVRGRKLA YFDLNGYWLA LNEEPDIPRN
     EIAHSYTHMA FTITEESFDE WYAHLEKHGV TILHGRDRSE RDKRSIYFID PDGHKFELHT
     GTLQDRLAYY RDEKHHMTFF E