THIO_BACSU
ID THIO_BACSU Reviewed; 104 AA.
AC P14949; O07960; Q45687;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Thioredoxin;
DE Short=Trx;
GN Name=trxA; Synonyms=trx; OrderedLocusNames=BSU28500;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2559145; DOI=10.1099/00221287-135-11-2931;
RA Chen N.-Y., Zhang J.-J., Paulus H.;
RT "Chromosomal location of the Bacillus subtilis aspartokinase II gene and
RT nucleotide sequence of the adjacent genes homologous to uvrC and trx of
RT Escherichia coli.";
RL J. Gen. Microbiol. 135:2931-2940(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
RA Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA Emmerson P.T., Harwood C.R.;
RT "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT chromosome containing genes responsible for stress responses, the
RT utilization of plant cell walls and primary metabolism.";
RL Microbiology 142:3067-3078(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP PROTEIN SEQUENCE OF 2-15.
RC STRAIN=168 / JH642;
RX PubMed=8755892; DOI=10.1128/jb.178.15.4611-4619.1996;
RA Graumann P., Schroeder K., Schmid R., Marahiel M.A.;
RT "Cold shock stress-induced proteins in Bacillus subtilis.";
RL J. Bacteriol. 178:4611-4619(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
RC STRAIN=168;
RA Riethdorf S., Winkler A., Voelker U., Ernst H., Scharf C., Hecker M.;
RL Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Participates in various redox reactions through the
CC reversible oxidation of its active center dithiol to a disulfide and
CC catalyzes dithiol-disulfide exchange reactions.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR EMBL; J03294; AAA87315.1; -; Genomic_DNA.
DR EMBL; Z75208; CAA99577.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14810.1; -; Genomic_DNA.
DR EMBL; X79976; CAA56300.1; -; Genomic_DNA.
DR EMBL; X99275; CAA67667.1; -; Genomic_DNA.
DR PIR; B37192; B37192.
DR RefSeq; NP_390728.1; NC_000964.3.
DR RefSeq; WP_003222500.1; NZ_JNCM01000036.1.
DR PDB; 2GZY; NMR; -; A=1-104.
DR PDB; 2GZZ; NMR; -; A=1-104.
DR PDB; 2IPA; NMR; -; A=1-104.
DR PDB; 2VOC; X-ray; 1.50 A; A/B=1-104.
DR PDBsum; 2GZY; -.
DR PDBsum; 2GZZ; -.
DR PDBsum; 2IPA; -.
DR PDBsum; 2VOC; -.
DR AlphaFoldDB; P14949; -.
DR BMRB; P14949; -.
DR SMR; P14949; -.
DR IntAct; P14949; 1.
DR MINT; P14949; -.
DR STRING; 224308.BSU28500; -.
DR jPOST; P14949; -.
DR PaxDb; P14949; -.
DR PRIDE; P14949; -.
DR EnsemblBacteria; CAB14810; CAB14810; BSU_28500.
DR GeneID; 50136691; -.
DR GeneID; 64304575; -.
DR GeneID; 938187; -.
DR KEGG; bsu:BSU28500; -.
DR PATRIC; fig|224308.179.peg.3095; -.
DR eggNOG; COG3118; Bacteria.
DR InParanoid; P14949; -.
DR OMA; QVGVAPK; -.
DR PhylomeDB; P14949; -.
DR BioCyc; BSUB:BSU28500-MON; -.
DR EvolutionaryTrace; P14949; -.
DR PRO; PR:P14949; -.
DR Proteomes; UP000001570; 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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Electron transport; Redox-active center; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8755892"
FT CHAIN 2..104
FT /note="Thioredoxin"
FT /id="PRO_0000120076"
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 STRAND 3..6
FT /evidence="ECO:0007829|PDB:2GZZ"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:2VOC"
FT HELIX 11..15
FT /evidence="ECO:0007829|PDB:2VOC"
FT STRAND 16..25
FT /evidence="ECO:0007829|PDB:2VOC"
FT HELIX 30..34
FT /evidence="ECO:0007829|PDB:2VOC"
FT HELIX 35..46
FT /evidence="ECO:0007829|PDB:2VOC"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:2VOC"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:2VOC"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:2VOC"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:2VOC"
FT STRAND 71..79
FT /evidence="ECO:0007829|PDB:2VOC"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:2VOC"
FT HELIX 93..101
FT /evidence="ECO:0007829|PDB:2VOC"
SQ SEQUENCE 104 AA; 11393 MW; B2989161062C264D CRC64;
MAIVKATDQS FSAETSEGVV LADFWAPWCG PCKMIAPVLE ELDQEMGDKL KIVKIDVDEN
QETAGKYGVM SIPTLLVLKD GEVVETSVGF KPKEALQELV NKHL
