ID   GSTB_ECOL6              Reviewed;         208 AA.
AC   P0ACA8; P75805; Q9R7R4;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=Glutathione S-transferase GstB;
DE            EC=2.5.1.18;
GN   Name=gstB; OrderedLocusNames=c0923;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles. {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN79396.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN79396.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001295292.1; NZ_CP051263.1.
DR   AlphaFoldDB; P0ACA8; -.
DR   SMR; P0ACA8; -.
DR   STRING; 199310.c0923; -.
DR   GeneID; 75204697; -.
DR   KEGG; ecc:c0923; -.
DR   eggNOG; COG0625; Bacteria.
DR   HOGENOM; CLU_011226_6_2_6; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR44051:SF10; GLUTATHIONE S-TRANSFERASE GSTA; 1.
DR   PANTHER; PTHR44051; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDG01150; Main.1:_Beta-like; 1.
DR   SFLD; SFLDG00358; Main_(cytGST); 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Transferase.
FT   CHAIN           1..208
FT                   /note="Glutathione S-transferase GstB"
FT                   /id="PRO_0000186019"
FT   DOMAIN          1..83
FT                   /note="GST N-terminal"
FT   DOMAIN          88..208
FT                   /note="GST C-terminal"
FT   BINDING         12
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         39
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         53
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         67..68
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   208 AA;  23713 MW;  8AD199E313B05094 CRC64;
     MITLWGRNNS TNVKKVLLTL EELELPYEQI LAGREFGINH DADFLAMNPN GLVPLLRDDE
     SDLILWESNA IVRYLAAQYG QKRLWIDSPA RRAEAEKWMD WANQTLSNAH RGILMGLVRT
     PPEERDQAAI DASCKECDAL FALLDAELAK VKWFSGDEFG VGDIAIAPFI YNLFNVGLTW
     TPRPNLQRWY QQLTERPAVR KVVMIPVS
//