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Database: UniProt
Entry: M1PJ75_BACTU
LinkDB: M1PJ75_BACTU
Original site: M1PJ75_BACTU 
ID   M1PJ75_BACTU            Unreviewed;       138 AA.
AC   M1PJ75;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Metallothiol transferase FosB {ECO:0000256|HAMAP-Rule:MF_01512};
DE            EC=2.5.1.- {ECO:0000256|HAMAP-Rule:MF_01512};
DE   AltName: Full=Fosfomycin resistance protein {ECO:0000256|HAMAP-Rule:MF_01512};
GN   Name=fosB {ECO:0000256|HAMAP-Rule:MF_01512};
GN   ORFNames=H175_ch2010 {ECO:0000313|EMBL:AGG00723.1};
OS   Bacillus thuringiensis serovar thuringiensis str. IS5056.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1286404 {ECO:0000313|EMBL:AGG00723.1, ECO:0000313|Proteomes:UP000011719};
RN   [1] {ECO:0000313|EMBL:AGG00723.1, ECO:0000313|Proteomes:UP000011719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IS5056 {ECO:0000313|EMBL:AGG00723.1};
RX   PubMed=23516221;
RA   Murawska E., Fiedoruk K., Bideshi D.K., Swiecicka I.;
RT   "Complete genome sequence of Bacillus thuringiensis subsp. thuringiensis
RT   strain IS5056, an isolate highly toxic to Trichoplusia ni.";
RL   Genome Announc. 1:E0010813-E0010813(2013).
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:0000256|HAMAP-Rule:MF_01512}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01512};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01512}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01512}.
CC   -!- SIMILARITY: Belongs to the fosfomycin resistance protein family. FosB
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01512}.
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DR   EMBL; CP004123; AGG00723.1; -; Genomic_DNA.
DR   RefSeq; WP_000943769.1; NC_020376.1.
DR   AlphaFoldDB; M1PJ75; -.
DR   SMR; M1PJ75; -.
DR   GeneID; 67466444; -.
DR   KEGG; btht:H175_ch2010; -.
DR   PATRIC; fig|1286404.3.peg.2033; -.
DR   HOGENOM; CLU_121356_0_0_9; -.
DR   Proteomes; UP000011719; 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; PTHR36113:SF1; FOSFOMYCIN RESISTANCE PROTEIN FOSX; 1.
DR   PANTHER; PTHR36113; LYASE, PUTATIVE-RELATED-RELATED; 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 {ECO:0000256|ARBA:ARBA00023251, ECO:0000256|HAMAP-
KW   Rule:MF_01512};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01512};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01512};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01512};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01512}.
FT   DOMAIN          4..119
FT                   /note="VOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51819"
FT   BINDING         7
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01512"
FT   BINDING         66
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01512"
FT   BINDING         115
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01512"
SQ   SEQUENCE   138 AA;  16474 MW;  FC9441FB0F04C057 CRC64;
     MLRGINHICF SVSNLENSIM FYEKVLEGEL LVKGRKLAYF NICGVWIALN EETHIPRNEI
     HQSYTHIAFS VEQEDFKCLI QRLEENDVHI LQGRERDVRD CESIYFVDPD GHKFEFHSGT
     LQDRLNYYRD EKPHMTFY
//
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