ID Q1RBG0_ECOUT Unreviewed; 201 AA.
AC Q1RBG0;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Glutathione S-transferase {ECO:0000313|EMBL:ABE07304.1};
DE EC=2.5.1.18 {ECO:0000313|EMBL:ABE07304.1};
GN Name=gst {ECO:0000313|EMBL:ABE07304.1};
GN OrderedLocusNames=UTI89_C1826 {ECO:0000313|EMBL:ABE07304.1};
OS Escherichia coli (strain UTI89 / UPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=364106 {ECO:0000313|EMBL:ABE07304.1, ECO:0000313|Proteomes:UP000001952};
RN [1] {ECO:0000313|EMBL:ABE07304.1, ECO:0000313|Proteomes:UP000001952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTI89 / UPEC {ECO:0000313|Proteomes:UP000001952};
RX PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA Chen S.L., Hung C.S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA Gordon J.I.;
RT "Identification of genes subject to positive selection in uropathogenic
RT strains of Escherichia coli: a comparative genomics approach.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000243; ABE07304.1; -; Genomic_DNA.
DR RefSeq; WP_000765765.1; NZ_CP064825.1.
DR AlphaFoldDB; Q1RBG0; -.
DR KEGG; eci:UTI89_C1826; -.
DR HOGENOM; CLU_011226_6_1_6; -.
DR Proteomes; UP000001952; 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:ABE07304.1}.
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; 22857 MW; BA99430C53BE49CA CRC64;
MKLFYKPGAC SLASHITLRE SGKDFTLVSV DLMKKRLENG DNYFAVNPKG QVPALLLDDG
TLLTEGVAIM QYLADSVPDR QLLAPVNSIS RYKTIEWLNY IATELHKGFT PLFRPDTPEE
YKSTVRAQLE KKLQYVNEAL KDEHWICGQR FTIADAYLFT VLRWAYAVKL NLEGLEHIAA
FMQRMAERPE VQDALSAEGL K
//
