ID   THIO_STAES              Reviewed;         104 AA.
AC   Q8CPL5;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Thioredoxin;
DE            Short=Trx;
GN   Name=trxA; OrderedLocusNames=SE_0838;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR   EMBL; AE015929; AAO04435.1; -; Genomic_DNA.
DR   RefSeq; NP_764393.1; NC_004461.1.
DR   RefSeq; WP_001830148.1; NZ_WBME01000035.1.
DR   AlphaFoldDB; Q8CPL5; -.
DR   SMR; Q8CPL5; -.
DR   STRING; 176280.SE_0838; -.
DR   EnsemblBacteria; AAO04435; AAO04435; SE_0838.
DR   GeneID; 50019024; -.
DR   KEGG; sep:SE_0838; -.
DR   PATRIC; fig|176280.10.peg.811; -.
DR   eggNOG; COG3118; Bacteria.
DR   HOGENOM; CLU_090389_10_2_9; -.
DR   OMA; QVGVAPK; -.
DR   Proteomes; UP000001411; Chromosome.
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   PIRSF; PIRSF000077; 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   3: Inferred from homology;
KW   Disulfide bond; Electron transport; Redox-active center; Transport.
FT   CHAIN           1..104
FT                   /note="Thioredoxin"
FT                   /id="PRO_0000120132"
FT   DOMAIN          2..104
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        29..32
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   104 AA;  11443 MW;  DBBCE61D2DA7E770 CRC64;
     MAIVKVTDSD FDSKIESGVK LVDFWATWCG PCKMIAPVLE ELAGDYDGKA DILKLDVDEN
     PSTAAKYEVM SIPTLIVFKD GEPVDKVVGF QPKENLAEVL DKHL