ID   THIO2_STRCO             Reviewed;         134 AA.
AC   Q9RD25;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 124.
DE   RecName: Full=Putative thioredoxin 2;
DE            Short=Trx-2;
GN   Name=trxC; OrderedLocusNames=SCO0885;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
RN   [2]
RP   INDUCTION.
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=11251822; DOI=10.1046/j.1365-2958.2001.02298.x;
RA   Paget M.S., Bae J.B., Hahn M.Y., Li W., Kleanthous C., Roe J.H.,
RA   Buttner M.J.;
RT   "Mutational analysis of RsrA, a zinc-binding anti-sigma factor with a
RT   thiol-disulphide redox switch.";
RL   Mol. Microbiol. 39:1036-1047(2001).
CC   -!- FUNCTION: Component of the thioredoxin-thioredoxin reductase system.
CC       Participates in various redox reactions through the reversible
CC       oxidation of its active center dithiol to a disulfide and catalyzes
CC       dithiol-disulfide exchange reactions (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- INDUCTION: Expressed from 2 promoters, 1 of which (trxCp1) is under
CC       control of SigR. Dramatically but transiently induced by the thiol-
CC       oxidizing agent diamide. In an rsrA mutant expression is constitutive
CC       and uninduced by diamide. {ECO:0000269|PubMed:11251822}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR   EMBL; AL939107; CAB62676.1; -; Genomic_DNA.
DR   RefSeq; NP_625184.1; NC_003888.3.
DR   RefSeq; WP_011027416.1; NZ_VNID01000004.1.
DR   AlphaFoldDB; Q9RD25; -.
DR   SMR; Q9RD25; -.
DR   STRING; 100226.SCO0885; -.
DR   GeneID; 1096308; -.
DR   KEGG; sco:SCO0885; -.
DR   PATRIC; fig|100226.15.peg.876; -.
DR   eggNOG; COG0526; Bacteria.
DR   HOGENOM; CLU_090389_10_4_11; -.
DR   InParanoid; Q9RD25; -.
DR   OMA; QRVDMIN; -.
DR   PhylomeDB; Q9RD25; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR01068; thioredoxin; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Disulfide bond; Electron transport; Redox-active center;
KW   Reference proteome; Transport.
FT   CHAIN           1..134
FT                   /note="Putative thioredoxin 2"
FT                   /id="PRO_0000423655"
FT   DOMAIN          3..106
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          115..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        119..134
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        31..34
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   134 AA;  14589 MW;  C526A78C04B4E444 CRC64;
     MTSTVELTKE NFDQTVTDNE FVLIDFWAEW CGPCKQFGPV YEKAAEANPD LVFGKVDTEA
     QPELAQAFGI SSIPTLMIVR EQVAVFAQPG ALPEAALTDV IGQARKLDMD EVRKAVAEQQ
     AQAGQNGQEG QEGQ