FOSA_PSEAE
ID FOSA_PSEAE Reviewed; 135 AA.
AC Q9I4K6;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Glutathione transferase FosA;
DE EC=2.5.1.18;
DE AltName: Full=Fosfomycin resistance protein;
GN Name=fosA; OrderedLocusNames=PA1129;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.19 ANGSTROMS) IN COMPLEX WITH FOSFOMYCIN,
RP FUNCTION, AND COFACTOR.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=12224946; DOI=10.1021/ja026879v;
RA Rife C.L., Pharris R.E., Newcomer M.E., Armstrong R.N.;
RT "Crystal structure of a genomically encoded fosfomycin resistance protein
RT (FosA) at 1.19 A resolution by MAD phasing off the L-III edge of Tl(+).";
RL J. Am. Chem. Soc. 124:11001-11003(2002).
CC -!- FUNCTION: Metalloglutathione transferase which confers resistance to
CC fosfomycin by catalyzing the addition of glutathione to fosfomycin.
CC {ECO:0000269|PubMed:12224946}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:12224946};
CC -!- ACTIVITY REGULATION: Requires the monovalent cation K(+) for optimal
CC activity.
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; AE004091; AAG04518.1; -; Genomic_DNA.
DR PIR; E83503; E83503.
DR RefSeq; NP_249820.1; NC_002516.2.
DR RefSeq; WP_003082280.1; NZ_QZGE01000006.1.
DR PDB; 1LQK; X-ray; 1.35 A; A/B=1-135.
DR PDB; 1LQO; X-ray; 2.00 A; A/B=1-135.
DR PDB; 1LQP; X-ray; 1.19 A; A/B=1-135.
DR PDB; 1NKI; X-ray; 0.95 A; A/B=1-135.
DR PDB; 1NNR; X-ray; 2.25 A; A/B=1-135.
DR PDBsum; 1LQK; -.
DR PDBsum; 1LQO; -.
DR PDBsum; 1LQP; -.
DR PDBsum; 1NKI; -.
DR PDBsum; 1NNR; -.
DR AlphaFoldDB; Q9I4K6; -.
DR SMR; Q9I4K6; -.
DR STRING; 287.DR97_805; -.
DR PaxDb; Q9I4K6; -.
DR PRIDE; Q9I4K6; -.
DR DNASU; 877785; -.
DR EnsemblBacteria; AAG04518; AAG04518; PA1129.
DR GeneID; 877785; -.
DR KEGG; ag:AAG04518; -.
DR KEGG; pae:PA1129; -.
DR PATRIC; fig|208964.12.peg.1174; -.
DR PseudoCAP; PA1129; -.
DR HOGENOM; CLU_121356_0_0_6; -.
DR InParanoid; Q9I4K6; -.
DR OMA; ELWLCLS; -.
DR PhylomeDB; Q9I4K6; -.
DR BioCyc; PAER208964:G1FZ6-1155-MON; -.
DR EvolutionaryTrace; Q9I4K6; -.
DR PRO; PR:Q9I4K6; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.10.180.10; -; 1.
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 Potassium; Reference proteome; Transferase; Zinc.
FT CHAIN 1..135
FT /note="Glutathione transferase FosA"
FT /id="PRO_0000164043"
FT DOMAIN 4..114
FT /note="VOC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT ACT_SITE 110
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT BINDING 7
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163,
FT ECO:0000269|PubMed:12224946, ECO:0007744|PDB:1LQK,
FT ECO:0007744|PDB:1LQP, ECO:0007744|PDB:1NKI,
FT ECO:0007744|PDB:1NNR"
FT BINDING 41
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT BINDING 64
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163,
FT ECO:0000269|PubMed:12224946, ECO:0007744|PDB:1LQK,
FT ECO:0007744|PDB:1LQP, ECO:0007744|PDB:1NKI,
FT ECO:0007744|PDB:1NNR"
FT BINDING 110
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163,
FT ECO:0000269|PubMed:12224946, ECO:0007744|PDB:1LQK,
FT ECO:0007744|PDB:1LQP, ECO:0007744|PDB:1NKI,
FT ECO:0007744|PDB:1NNR"
FT STRAND 2..13
FT /evidence="ECO:0007829|PDB:1NKI"
FT HELIX 15..24
FT /evidence="ECO:0007829|PDB:1NKI"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:1NKI"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:1NKI"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:1NKI"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:1NKI"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:1NKI"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:1NKI"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:1NKI"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:1NKI"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1NKI"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:1NKI"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:1NKI"
FT HELIX 116..125
FT /evidence="ECO:0007829|PDB:1NKI"
SQ SEQUENCE 135 AA; 15124 MW; 0D75F174291A2366 CRC64;
MLTGLNHLTL AVADLPASIA FYRDLLGFRL EARWDQGAYL ELGSLWLCLS REPQYGGPAA
DYTHYAFGIA AADFARFAAQ LRAHGVREWK QNRSEGDSFY FLDPDGHRLE AHVGDLRSRL
AACRQAPYAG MRFAD
