FOSB2_BACAN
ID FOSB2_BACAN Reviewed; 139 AA.
AC Q81W73; Q6HUC0; Q6KNK7;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Metallothiol transferase FosB 2 {ECO:0000255|HAMAP-Rule:MF_01512};
DE EC=2.5.1.- {ECO:0000255|HAMAP-Rule:MF_01512};
DE AltName: Full=Fosfomycin resistance protein 2 {ECO:0000255|HAMAP-Rule:MF_01512};
GN Name=fosB2 {ECO:0000255|HAMAP-Rule:MF_01512}; Synonyms=fosB-2;
GN OrderedLocusNames=BA_4109, GBAA_4109, BAS3818;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) 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; AE016879; AAP27834.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT33228.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT56119.1; -; Genomic_DNA.
DR RefSeq; NP_846348.1; NC_003997.3.
DR RefSeq; WP_000938987.1; NZ_WXXJ01000026.1.
DR RefSeq; YP_030068.1; NC_005945.1.
DR PDB; 4IR0; X-ray; 1.60 A; A/B=1-139.
DR PDB; 4JD1; X-ray; 1.70 A; A/B=1-139.
DR PDB; 5F6Q; X-ray; 1.52 A; A/B=1-139.
DR PDBsum; 4IR0; -.
DR PDBsum; 4JD1; -.
DR PDBsum; 5F6Q; -.
DR AlphaFoldDB; Q81W73; -.
DR SMR; Q81W73; -.
DR STRING; 260799.BAS3818; -.
DR DNASU; 1086311; -.
DR EnsemblBacteria; AAP27834; AAP27834; BA_4109.
DR EnsemblBacteria; AAT33228; AAT33228; GBAA_4109.
DR GeneID; 45023793; -.
DR KEGG; ban:BA_4109; -.
DR KEGG; bar:GBAA_4109; -.
DR KEGG; bat:BAS3818; -.
DR PATRIC; fig|198094.11.peg.4079; -.
DR eggNOG; COG0346; Bacteria.
DR HOGENOM; CLU_121356_0_0_9; -.
DR OMA; IPRNDIQ; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; 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 Reference proteome; Transferase.
FT CHAIN 1..139
FT /note="Metallothiol transferase FosB 2"
FT /id="PRO_0000164023"
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 7..13
FT /evidence="ECO:0007829|PDB:5F6Q"
FT HELIX 15..24
FT /evidence="ECO:0007829|PDB:5F6Q"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:5F6Q"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:5F6Q"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:5F6Q"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:5F6Q"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:5F6Q"
FT HELIX 73..85
FT /evidence="ECO:0007829|PDB:5F6Q"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:5F6Q"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:5F6Q"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:5F6Q"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:5F6Q"
FT HELIX 121..131
FT /evidence="ECO:0007829|PDB:5F6Q"
SQ SEQUENCE 139 AA; 16525 MW; E2F02F9F77690B4C CRC64;
MLQGINHICF SVSNLEKSIE FYQKILQAKL LVKGRKLAYF DLNGLWIALN VEEDIPRNEI
KQSYTHMAFT VTNEALDHLK EVLIQNDVNI LPGRERDERD QRSLYFTDPD GHKFEFHTGT
LQNRLEYYKE DKKHMTFYI
