FOSB_BACC1
ID FOSB_BACC1 Reviewed; 138 AA.
AC Q739M9;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=BCE_2111;
OS Bacillus cereus (strain ATCC 10987 / NRS 248).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=222523;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10987 / NRS 248;
RX PubMed=14960714; DOI=10.1093/nar/gkh258;
RA Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL Nucleic Acids Res. 32:977-988(2004).
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; AE017194; AAS41032.1; -; Genomic_DNA.
DR RefSeq; WP_000931692.1; NC_003909.8.
DR PDB; 4JH1; X-ray; 1.55 A; A/B=1-138.
DR PDB; 4JH2; X-ray; 1.27 A; A/B=1-138.
DR PDB; 4JH3; X-ray; 1.50 A; A/B=1-138.
DR PDB; 4JH4; X-ray; 1.90 A; A/B=1-138.
DR PDB; 4JH5; X-ray; 1.77 A; A/B=1-138.
DR PDB; 4JH6; X-ray; 1.32 A; A/B=1-138.
DR PDB; 4JH7; X-ray; 1.55 A; A/B=1-138.
DR PDB; 4JH8; X-ray; 1.41 A; A/B=1-138.
DR PDB; 4JH9; X-ray; 1.77 A; A/B=1-138.
DR PDBsum; 4JH1; -.
DR PDBsum; 4JH2; -.
DR PDBsum; 4JH3; -.
DR PDBsum; 4JH4; -.
DR PDBsum; 4JH5; -.
DR PDBsum; 4JH6; -.
DR PDBsum; 4JH7; -.
DR PDBsum; 4JH8; -.
DR PDBsum; 4JH9; -.
DR AlphaFoldDB; Q739M9; -.
DR SMR; Q739M9; -.
DR EnsemblBacteria; AAS41032; AAS41032; BCE_2111.
DR GeneID; 59157763; -.
DR KEGG; bca:BCE_2111; -.
DR HOGENOM; CLU_121356_0_0_9; -.
DR OMA; ELWLCLS; -.
DR Proteomes; UP000002527; 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 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Cytoplasm; Magnesium; Metal-binding;
KW Transferase.
FT CHAIN 1..138
FT /note="Metallothiol transferase FosB"
FT /id="PRO_0000164025"
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"
FT STRAND 4..13
FT /evidence="ECO:0007829|PDB:4JH2"
FT HELIX 15..24
FT /evidence="ECO:0007829|PDB:4JH2"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:4JH2"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:4JH2"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:4JH2"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:4JH3"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:4JH2"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:4JH2"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:4JH2"
FT HELIX 76..85
FT /evidence="ECO:0007829|PDB:4JH2"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:4JH8"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:4JH2"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:4JH2"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:4JH2"
FT HELIX 121..131
FT /evidence="ECO:0007829|PDB:4JH2"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:4JH2"
SQ SEQUENCE 138 AA; 16466 MW; 8F5BEA8D18767182 CRC64;
MLNGINHLCF SVSNLEDSIE FYEKVLEGEL LVRGRKLAYF NICGVWVALN EEIHIPRNEI
YQSYTHIAFS VEQKDFESLL QRLEENDVHI LKGRERDVRD CESIYFVDPD GHKFEFHSGT
LQDRLNYYRE DKPHMTFY
