FOSB_BACSU
ID FOSB_BACSU Reviewed; 144 AA.
AC O31817;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Metallothiol transferase FosB;
DE EC=2.5.1.-;
DE AltName: Full=Fosfomycin resistance protein;
GN Name=fosB; Synonyms=yndN; OrderedLocusNames=BSU17840;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP CHARACTERIZATION.
RC STRAIN=168;
RX PubMed=11244082; DOI=10.1128/jb.183.7.2380-2383.2001;
RA Cao M., Bernat B.A., Wang Z., Armstrong R.N., Helmann J.D.;
RT "FosB, a cysteine-dependent fosfomycin resistance protein under the control
RT of sigma(W), an extracytoplasmic-function sigma factor in Bacillus
RT subtilis.";
RL J. Bacteriol. 183:2380-2383(2001).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Expression is sigma W-dependent.
CC -!- SIMILARITY: Belongs to the fosfomycin resistance protein family. FosB
CC subfamily. {ECO:0000305}.
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DR EMBL; AL009126; CAB13668.1; -; Genomic_DNA.
DR PIR; E69890; E69890.
DR RefSeq; NP_389667.1; NC_000964.3.
DR RefSeq; WP_003231604.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O31817; -.
DR SMR; O31817; -.
DR STRING; 224308.BSU17840; -.
DR PaxDb; O31817; -.
DR DNASU; 938817; -.
DR EnsemblBacteria; CAB13668; CAB13668; BSU_17840.
DR GeneID; 938817; -.
DR KEGG; bsu:BSU17840; -.
DR PATRIC; fig|224308.179.peg.1944; -.
DR eggNOG; COG0346; Bacteria.
DR InParanoid; O31817; -.
DR OMA; ELWLCLS; -.
DR PhylomeDB; O31817; -.
DR BioCyc; BSUB:BSU17840-MON; -.
DR Proteomes; UP000001570; 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 Antibiotic resistance; Cytoplasm; Magnesium; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..144
FT /note="Metallothiol transferase FosB"
FT /id="PRO_0000164032"
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:0000250"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 144 AA; 17172 MW; EC4B5F8C1F718E18 CRC64;
MEIKGINHLL FSVSHLDTSI DFYQKVFGAK LLVKGRTTAY FDMNGIWLAL NEEPDIPRND
IKLSYTHIAF TIEDHEFEEM SAKLKRLHVN ILPGRERDER DRKSIYFTDP DGHKFEFHTG
TLQDRLRYYK QEKTHMHFYD ETAF
