ID   Y1296_STRMU             Reviewed;         263 AA.
AC   Q8DTN7;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Uncharacterized GST-like protein SMU_1296;
DE            EC=2.-.-.-;
GN   OrderedLocusNames=SMU_1296;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN   [2]
RP   OPERON STRUCTURE.
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=19429620; DOI=10.1128/jb.00184-09;
RA   Zhang J., Biswas I.;
RT   "3'-Phosphoadenosine-5'-phosphate phosphatase activity is required for
RT   superoxide stress tolerance in Streptococcus mutans.";
RL   J. Bacteriol. 191:4330-4340(2009).
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Part of the SMU_1296-SMU_1298 operon.
CC       {ECO:0000305|PubMed:19429620}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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DR   EMBL; AE014133; AAN58973.1; -; Genomic_DNA.
DR   RefSeq; NP_721667.1; NC_004350.2.
DR   RefSeq; WP_002263150.1; NC_004350.2.
DR   AlphaFoldDB; Q8DTN7; -.
DR   SMR; Q8DTN7; -.
DR   STRING; 210007.SMU_1296; -.
DR   PRIDE; Q8DTN7; -.
DR   EnsemblBacteria; AAN58973; AAN58973; SMU_1296.
DR   GeneID; 66817311; -.
DR   KEGG; smu:SMU_1296; -.
DR   PATRIC; fig|210007.7.peg.1161; -.
DR   eggNOG; COG0625; Bacteria.
DR   HOGENOM; CLU_011226_14_4_9; -.
DR   OMA; SGSIMQY; -.
DR   PhylomeDB; Q8DTN7; -.
DR   Proteomes; UP000002512; Chromosome.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
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; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 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..263
FT                   /note="Uncharacterized GST-like protein SMU_1296"
FT                   /id="PRO_0000419757"
FT   DOMAIN          44..131
FT                   /note="GST N-terminal"
FT   DOMAIN          134..263
FT                   /note="GST C-terminal"
SQ   SEQUENCE   263 AA;  29992 MW;  14F9B96102A23083 CRC64;
     MSYYIPPKVW SAEESNQGKF SAINRPTAGS RFDQKLPQGD KPLQVYSLGT PNGLKVAVML
     EELRELGVKE ADYDLFKISI MDGDQFGSDF VAINPNSKIP SLLDKSNREA IRVFESGSIL
     LYLADKFNHL IPVDWAQRTE VLNWLFWQMG AAPFVGGGFG HFFSYAPEKL EYPINRFTME
     TKRQLDLLNK ELANKPYIAG EDYTIADIAI WSWYGRLAQD ALYEGAYKFL ALGTYQHLLD
     WTERIAQRPA VKRALEVDYK AIK