THIO_STAA8
ID THIO_STAA8 Reviewed; 104 AA.
AC Q2FZD2;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Thioredoxin;
DE Short=Trx;
GN Name=trxA; OrderedLocusNames=SAOUHSC_01100;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP INDUCTION.
RX PubMed=14702300; DOI=10.1128/jb.186.2.326-334.2004;
RA Uziel O., Borovok I., Schreiber R., Cohen G., Aharonowitz Y.;
RT "Transcriptional regulation of the Staphylococcus aureus thioredoxin and
RT thioredoxin reductase genes in response to oxygen and disulfide stress.";
RL J. Bacteriol. 186:326-334(2004).
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 -!- INDUCTION: Induced by diamide, tau-butyl hydroperoxide, and menadione.
CC However, at concentrations above 0.5 mM, menadione has an inhibitory
CC effect on induction of trxA transcription.
CC {ECO:0000269|PubMed:14702300}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR EMBL; CP000253; ABD30214.1; -; Genomic_DNA.
DR RefSeq; WP_001018928.1; NZ_LS483365.1.
DR RefSeq; YP_499644.1; NC_007795.1.
DR AlphaFoldDB; Q2FZD2; -.
DR SMR; Q2FZD2; -.
DR STRING; 1280.SAXN108_1140; -.
DR EnsemblBacteria; ABD30214; ABD30214; SAOUHSC_01100.
DR GeneID; 3920742; -.
DR GeneID; 66839339; -.
DR KEGG; sao:SAOUHSC_01100; -.
DR PATRIC; fig|93061.5.peg.1008; -.
DR eggNOG; COG3118; Bacteria.
DR HOGENOM; CLU_090389_10_2_9; -.
DR OMA; QVGVAPK; -.
DR PRO; PR:Q2FZD2; -.
DR Proteomes; UP000008816; 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; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Disulfide bond; Electron transport; Redox-active center;
KW Reference proteome; Transport.
FT CHAIN 1..104
FT /note="Thioredoxin"
FT /id="PRO_0000267205"
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
