THIO_STAAU
ID THIO_STAAU Reviewed; 104 AA.
AC P0A0K6; Q9ZEH4;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Thioredoxin;
DE Short=Trx;
GN Name=trxA;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=ATCC 9144 / DSM 683 / NCIB 6571 / NCTC 6571 / NRRL B-314 / Oxford;
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: Expressed in both aerobic and anaerobic conditions.
CC {ECO:0000269|PubMed:14702300}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR EMBL; AJ223480; CAA11404.1; -; Genomic_DNA.
DR RefSeq; WP_001018928.1; NZ_WYDB01000003.1.
DR PDB; 2O7K; X-ray; 2.20 A; A=1-104.
DR PDB; 2O85; X-ray; 2.20 A; A=1-104.
DR PDB; 2O87; X-ray; 2.40 A; A=2-104.
DR PDB; 2O89; X-ray; 2.55 A; A=1-104.
DR PDB; 3DIE; X-ray; 1.85 A; A/B=1-104.
DR PDBsum; 2O7K; -.
DR PDBsum; 2O85; -.
DR PDBsum; 2O87; -.
DR PDBsum; 2O89; -.
DR PDBsum; 3DIE; -.
DR AlphaFoldDB; P0A0K6; -.
DR SMR; P0A0K6; -.
DR GeneID; 66839339; -.
DR OMA; QVGVAPK; -.
DR EvolutionaryTrace; P0A0K6; -.
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 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Electron transport; Redox-active center;
KW Transport.
FT CHAIN 1..104
FT /note="Thioredoxin"
FT /id="PRO_0000120131"
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"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:3DIE"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:3DIE"
FT STRAND 17..25
FT /evidence="ECO:0007829|PDB:3DIE"
FT HELIX 30..45
FT /evidence="ECO:0007829|PDB:3DIE"
FT TURN 46..49
FT /evidence="ECO:0007829|PDB:3DIE"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:3DIE"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:3DIE"
FT HELIX 61..66
FT /evidence="ECO:0007829|PDB:3DIE"
FT STRAND 71..79
FT /evidence="ECO:0007829|PDB:3DIE"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:3DIE"
FT HELIX 93..101
FT /evidence="ECO:0007829|PDB:3DIE"
SQ SEQUENCE 104 AA; 11440 MW; FE61559DB27B3920 CRC64;
MAIVKVTDAD FDSKVESGVQ LVDFWATWCG PCKMIAPVLE ELAADYEGKA DILKLDVDEN
PSTAAKYEVM SIPTLIVFKD GQPVDKVVGF QPKENLAEVL DKHL
