ID   THIO_STAAM              Reviewed;         104 AA.
AC   P0A0K4; Q9ZEH4;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Thioredoxin;
DE            Short=Trx;
GN   Name=trxA; OrderedLocusNames=SAV1145;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(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   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR   EMBL; BA000017; BAB57307.1; -; Genomic_DNA.
DR   RefSeq; WP_001018928.1; NC_002758.2.
DR   AlphaFoldDB; P0A0K4; -.
DR   SMR; P0A0K4; -.
DR   World-2DPAGE; 0002:P0A0K4; -.
DR   PaxDb; P0A0K4; -.
DR   EnsemblBacteria; BAB57307; BAB57307; SAV1145.
DR   GeneID; 66839339; -.
DR   KEGG; sav:SAV1145; -.
DR   HOGENOM; CLU_090389_10_2_9; -.
DR   OMA; QVGVAPK; -.
DR   PhylomeDB; P0A0K4; -.
DR   BioCyc; SAUR158878:SAV_RS06165-MON; -.
DR   Proteomes; UP000002481; 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_0000120126"
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;  11440 MW;  FE61559DB27B3920 CRC64;
     MAIVKVTDAD FDSKVESGVQ LVDFWATWCG PCKMIAPVLE ELAADYEGKA DILKLDVDEN
     PSTAAKYEVM SIPTLIVFKD GQPVDKVVGF QPKENLAEVL DKHL