ID   GSTB_ECOLI              Reviewed;         208 AA.
AC   P0ACA7; P75805; Q9R7R4;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   02-SEP-2026, entry version 136.
DE   RecName: Full=Glutathione S-transferase GstB;
DE            EC=2.5.1.18;
GN   Name=gstB; Synonyms=yliJ; OrderedLocusNames=b0838, JW0822;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION
RP   PHENOTYPE, AND GENE NAME.
RX   PubMed=20921376; DOI=10.1073/pnas.1007559107;
RA   Desai K.K., Miller B.G.;
RT   "Recruitment of genes and enzymes conferring resistance to the nonnatural
RT   toxin bromoacetate.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:17968-17973(2010).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles. Catalyzes the
CC       glutathione-dependent dehalogenation of bromoacetate.
CC       {ECO:0000269|PubMed:20921376}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=RX + glutathione = an S-substituted glutathione + a halide
CC         anion + 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         Evidence={ECO:0000269|PubMed:20921376};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=5 mM for bromoacetate {ECO:0000269|PubMed:20921376};
CC   -!- INTERACTION:
CC       P0ACA7; P0ACA7: gstB; NbExp=2; IntAct=EBI-1120568, EBI-1120568;
CC       P0ACA7; P06987: hisB; NbExp=4; IntAct=EBI-1120568, EBI-1126930;
CC   -!- DISRUPTION PHENOTYPE: Mutants are hypersensitive to bromoacetate.
CC       {ECO:0000269|PubMed:20921376}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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DR   EMBL; U00096; AAC73925.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35541.1; -; Genomic_DNA.
DR   RefSeq; NP_415359.4; NC_000913.3.
DR   RefSeq; WP_001295292.1; NZ_CP009789.1.
DR   AlphaFoldDB; P0ACA7; -.
DR   SMR; P0ACA7; -.
DR   BioGRID; 4262824; 15.
DR   BioGRID; 849843; 2.
DR   DIP; DIP-48220N; -.
DR   FunCoup; P0ACA7; 166.
DR   IntAct; P0ACA7; 2.
DR   STRING; 511145.b0838; -.
DR   jPOST; P0ACA7; -.
DR   PaxDb; 511145-b0838; -.
DR   EnsemblBacteria; AAC73925; AAC73925; b0838.
DR   GeneID; 75170907; -.
DR   GeneID; 75204697; -.
DR   GeneID; 945469; -.
DR   KEGG; ecj:JW0822; -.
DR   KEGG; eco:b0838; -.
DR   KEGG; ecoc:C3026_05245; -.
DR   PATRIC; fig|1411691.4.peg.1440; -.
DR   EchoBASE; EB3254; -.
DR   eggNOG; COG0625; Bacteria.
DR   HOGENOM; CLU_011226_6_2_6; -.
DR   InParanoid; P0ACA7; -.
DR   OMA; QGEKWMD; -.
DR   OrthoDB; 5958450at2; -.
DR   PhylomeDB; P0ACA7; -.
DR   BioCyc; EcoCyc:G6438-MONOMER; -.
DR   BioCyc; MetaCyc:G6438-MONOMER; -.
DR   SABIO-RK; P0ACA7; -.
DR   PRO; PR:P0ACA7; -.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0030611; F:arsenate reductase activity; IDA:EcoCyc.
DR   GO; GO:0004364; F:glutathione transferase activity; IDA:EcoCyc.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   FunFam; 3.40.30.10:FF:000039; Glutathione S-transferase domain; 1.
DR   FunFam; 1.20.1050.10:FF:000013; Glutathione S-transferase GstB; 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:SF19; DISULFIDE-BOND OXIDOREDUCTASE YFCG; 1.
DR   PANTHER; PTHR44051; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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   1: Evidence at protein level;
KW   Reference proteome; Transferase.
FT   CHAIN           1..208
FT                   /note="Glutathione S-transferase GstB"
FT                   /id="PRO_0000186018"
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
//