ID   B7NB89_ECOLU            Unreviewed;       201 AA.
AC   B7NB89;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Glutathionine S-transferase {ECO:0000313|EMBL:CAR13123.1};
DE            EC=2.5.1.18 {ECO:0000313|EMBL:CAR13123.1};
GN   Name=gst {ECO:0000313|EMBL:CAR13123.1};
GN   OrderedLocusNames=ECUMN_1926 {ECO:0000313|EMBL:CAR13123.1};
OS   Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585056 {ECO:0000313|EMBL:CAR13123.1, ECO:0000313|Proteomes:UP000007097};
RN   [1] {ECO:0000313|Proteomes:UP000007097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMN026 / ExPEC {ECO:0000313|Proteomes:UP000007097};
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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DR   EMBL; CU928163; CAR13123.1; -; Genomic_DNA.
DR   RefSeq; WP_000765742.1; NC_011751.1.
DR   RefSeq; YP_002412655.1; NC_011751.1.
DR   AlphaFoldDB; B7NB89; -.
DR   STRING; 585056.ECUMN_1926; -.
DR   KEGG; eum:ECUMN_1926; -.
DR   PATRIC; fig|585056.7.peg.2109; -.
DR   HOGENOM; CLU_011226_6_1_6; -.
DR   Proteomes; UP000007097; Chromosome.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   CDD; cd03188; GST_C_Beta; 1.
DR   CDD; cd03057; GST_N_Beta; 1.
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; IPR040079; Glutathione_S-Trfase.
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; PF13409; GST_N_2; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG01150; Main.1:_Beta-like; 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   4: Predicted;
KW   Transferase {ECO:0000313|EMBL:CAR13123.1}.
FT   DOMAIN          1..81
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          87..201
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   201 AA;  22854 MW;  62F741A093B044E3 CRC64;
     MKLFYKPGAC SLASHITLRE SGKDFTLVSV DLMKKRLENG DDYFAVNPKG QVPALLLDDG
     TLLTEGVAIM QYLADSVPDR QLLAPVNSIS RYKTIEWLNY IATELHKGFT PLFRPDTPEE
     YKPTVRAQLE KKLQYVNDAL KDEHWICGQR FTIADAYLFT VLRWAYAVKL NLEGLEHIAA
     FMQRMAERPE VQDALSAEGL K
//