FOSB_STAAN
ID FOSB_STAAN Reviewed; 139 AA.
AC P60864; Q99RU0;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=SA2124;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(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 {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; BA000018; BAB43425.1; -; Genomic_DNA.
DR PIR; H90032; H90032.
DR RefSeq; WP_000920239.1; NC_002745.2.
DR PDB; 4NAY; X-ray; 1.42 A; A=2-139.
DR PDB; 4NAZ; X-ray; 1.15 A; A=2-139.
DR PDB; 4NB0; X-ray; 1.62 A; A/B=2-139.
DR PDB; 4NB1; X-ray; 1.80 A; A/B=1-139.
DR PDB; 4NB2; X-ray; 1.89 A; A/B=1-139.
DR PDBsum; 4NAY; -.
DR PDBsum; 4NAZ; -.
DR PDBsum; 4NB0; -.
DR PDBsum; 4NB1; -.
DR PDBsum; 4NB2; -.
DR AlphaFoldDB; P60864; -.
DR SMR; P60864; -.
DR EnsemblBacteria; BAB43425; BAB43425; BAB43425.
DR KEGG; sau:SA2124; -.
DR HOGENOM; CLU_121356_0_0_9; -.
DR OMA; ELWLCLS; -.
DR BioCyc; MetaCyc:MON-19022; -.
DR Proteomes; UP000000751; 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 Transferase.
FT CHAIN 1..139
FT /note="Metallothiol transferase FosB"
FT /id="PRO_0000164036"
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:4NAZ"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:4NAZ"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:4NAZ"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:4NAZ"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:4NAZ"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:4NAZ"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:4NAZ"
FT HELIX 76..85
FT /evidence="ECO:0007829|PDB:4NAZ"
FT TURN 95..101
FT /evidence="ECO:0007829|PDB:4NB0"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:4NAZ"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:4NAZ"
FT HELIX 121..131
FT /evidence="ECO:0007829|PDB:4NAZ"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:4NB0"
SQ SEQUENCE 139 AA; 16648 MW; 6C5AF119A5E08062 CRC64;
MLKSINHICF SVRNLNDSIH FYRDILLGKL LLTGKKTAYF ELAGLWIALN EEKDIPRNEI
HFSYTHIAFT IDDSEFKYWH QRLKDNNVNI LEGRVRDIRD RQSIYFTDPD GHKLELHTGT
LENRLNYYKE AKPHMTFYK
