FOSX_LISMO
ID FOSX_LISMO Reviewed; 133 AA.
AC Q8Y6I2;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Fosfomycin resistance protein FosX;
GN Name=fosX; OrderedLocusNames=lmo1702;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [2]
RP FUNCTION, COFACTOR, AND MUTAGENESIS OF GLU-44.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=14677948; DOI=10.1021/ja039307z;
RA Fillgrove K.L., Pakhomova S., Newcomer M.E., Armstrong R.N.;
RT "Mechanistic diversity of fosfomycin resistance in pathogenic
RT microorganisms.";
RL J. Am. Chem. Soc. 125:15730-15731(2003).
CC -!- FUNCTION: Catalyzes the hydration of fosfomycin.
CC {ECO:0000269|PubMed:14677948}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:14677948};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the fosfomycin resistance protein family.
CC {ECO:0000305}.
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DR EMBL; AL591981; CAC99780.1; -; Genomic_DNA.
DR PIR; AF1287; AF1287.
DR RefSeq; NP_465227.1; NC_003210.1.
DR RefSeq; WP_010989789.1; NZ_CP023861.1.
DR PDB; 2P7K; X-ray; 3.30 A; A/B=1-133.
DR PDB; 2P7L; X-ray; 2.20 A; A/B/C/D/E/F=1-133.
DR PDB; 2P7M; X-ray; 1.85 A; A/B/C/D/E/F=1-133.
DR PDB; 2P7O; X-ray; 1.44 A; A/B=1-133.
DR PDB; 2P7P; X-ray; 2.17 A; A/B/C/D/E/F=1-133.
DR PDBsum; 2P7K; -.
DR PDBsum; 2P7L; -.
DR PDBsum; 2P7M; -.
DR PDBsum; 2P7O; -.
DR PDBsum; 2P7P; -.
DR AlphaFoldDB; Q8Y6I2; -.
DR SMR; Q8Y6I2; -.
DR STRING; 169963.lmo1702; -.
DR PaxDb; Q8Y6I2; -.
DR EnsemblBacteria; CAC99780; CAC99780; CAC99780.
DR GeneID; 985982; -.
DR KEGG; lmo:lmo1702; -.
DR PATRIC; fig|169963.11.peg.1745; -.
DR eggNOG; COG0346; Bacteria.
DR HOGENOM; CLU_121356_1_0_9; -.
DR OMA; ELWLCLS; -.
DR PhylomeDB; Q8Y6I2; -.
DR BioCyc; LMON169963:LMO1702-MON; -.
DR EvolutionaryTrace; Q8Y6I2; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR CDD; cd08364; FosX; 1.
DR Gene3D; 3.10.180.10; -; 1.
DR InterPro; IPR037434; FosX.
DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
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; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..133
FT /note="Fosfomycin resistance protein FosX"
FT /id="PRO_0000164046"
FT DOMAIN 4..122
FT /note="VOC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT ACT_SITE 44
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT BINDING 7
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT MUTAGEN 44
FT /note="E->G: Almost no activity."
FT /evidence="ECO:0000269|PubMed:14677948"
FT STRAND 4..13
FT /evidence="ECO:0007829|PDB:2P7O"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:2P7O"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:2P7M"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:2P7P"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:2P7L"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:2P7O"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:2P7O"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:2P7O"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:2P7O"
FT HELIX 79..89
FT /evidence="ECO:0007829|PDB:2P7O"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:2P7K"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:2P7O"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:2P7O"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:2P7O"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:2P7L"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:2P7O"
SQ SEQUENCE 133 AA; 15655 MW; 3E5AF0E9B6A6F18A CRC64;
MISGLSHITL IVKDLNKTTT FLREIFNAEE IYSSGDQTFS LSKEKFFLIA GLWICIMEGD
SLQEQTYNHI AFRIQSEEVD EYIERIKSLG VEIKPERPRV EGEGRSIYFY DFDNHLFELH
AGTLEERLKR YHE
