FOSB_GEOTN
ID FOSB_GEOTN Reviewed; 140 AA.
AC A4IS40;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=GTNG_2799;
OS Geobacillus thermodenitrificans (strain NG80-2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=420246;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NG80-2;
RX PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA Han W., Peng X., Liu R., Wang L.;
RT "Genome and proteome of long-chain alkane degrading Geobacillus
RT thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
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; CP000557; ABO68144.1; -; Genomic_DNA.
DR RefSeq; WP_008881005.1; NC_009328.1.
DR AlphaFoldDB; A4IS40; -.
DR SMR; A4IS40; -.
DR STRING; 420246.GTNG_2799; -.
DR EnsemblBacteria; ABO68144; ABO68144; GTNG_2799.
DR KEGG; gtn:GTNG_2799; -.
DR eggNOG; COG0346; Bacteria.
DR HOGENOM; CLU_121356_0_0_9; -.
DR OMA; IPRNDIQ; -.
DR OrthoDB; 1984437at2; -.
DR Proteomes; UP000001578; 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; Transferase.
FT CHAIN 1..140
FT /note="Metallothiol transferase FosB"
FT /id="PRO_0000296658"
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 140 AA; 16490 MW; 905250EE8BED5608 CRC64;
MRIGGINHLT FSVSDLEKSI HFYQNVFGAK LLVKGRNLAY FDLNGIWLAL NVQQDIPRND
IQHSYTHIAF SVKEEDFDHV VEKLKELGVN ILPGRERDER DKRSVYFTDP DGHKFEFHTG
TLNDRLSYYK SEMHHMQFFD
