ID FOSB_STAES Reviewed; 142 AA.
AC P59291;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 1.
DT 27-MAR-2024, entry version 109.
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=SE_0231;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(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; AE015929; AAO03828.1; -; Genomic_DNA.
DR RefSeq; NP_763786.1; NC_004461.1.
DR RefSeq; WP_002437790.1; NZ_WBME01000011.1.
DR AlphaFoldDB; P59291; -.
DR SMR; P59291; -.
DR KEGG; sep:SE_0231; -.
DR PATRIC; fig|176280.10.peg.210; -.
DR eggNOG; COG0346; Bacteria.
DR HOGENOM; CLU_121356_0_0_9; -.
DR OrthoDB; 192739at2; -.
DR Proteomes; UP000001411; 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 CDD; cd08363; FosB; 1.
DR Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 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 PANTHER; PTHR21366:SF22; GLYOXALASE DOMAIN-CONTAINING PROTEIN 5; 1.
DR PANTHER; PTHR21366; GLYOXALASE FAMILY PROTEIN; 1.
DR Pfam; PF00903; Glyoxalase; 1.
DR SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 1.
DR PROSITE; PS51819; VOC; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; Cytoplasm; Magnesium; Metal-binding; Transferase.
FT CHAIN 1..142
FT /note="Metallothiol transferase FosB"
FT /id="PRO_0000164039"
FT DOMAIN 5..120
FT /note="VOC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT ACT_SITE 116
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01512"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01512"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01512"
SQ SEQUENCE 142 AA; 16844 MW; 036502BE1C6594DF CRC64;
MEITSVNHIC FSVSDLNTSI QFYKDILHGD LLVSGRTTAY LTIGHTWIAL NQEKNIPRNE
ISHSYTHIAF SIDEEDFQQW IQWLKENQVN ILKGRPRDIK DKKSIYFTDP DGHKIELHTG
TLKDRMEYYK CENTHMQFYD EF
//
