ID   THIO_CHLCV              Reviewed;         102 AA.
AC   P52227;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Thioredoxin;
DE            Short=Trx;
GN   Name=trxA; Synonyms=trx; OrderedLocusNames=CCA_00080;
OS   Chlamydia caviae (strain ATCC VR-813 / DSM 19441 / 03DC25 / GPIC)
OS   (Chlamydophila caviae).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=227941;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC VR-813 / DSM 19441 / 03DC25 / GPIC;
RX   PubMed=8936321; DOI=10.1099/00221287-142-4-945;
RA   Rockey D.D., Chesebro B.B., Heinzen R.A., Hackstadt T.;
RT   "A 28 kDa major immunogen of Chlamydia psittaci shares identity with Mip
RT   proteins of Legionella spp. and Chlamydia trachomatis-cloning and
RT   characterization of the C. psittaci mip-like gene.";
RL   Microbiology 142:945-953(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-813 / DSM 19441 / 03DC25 / GPIC;
RX   PubMed=12682364; DOI=10.1093/nar/gkg321;
RA   Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T.,
RA   Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A.,
RA   Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O.,
RA   Salzberg S.L., Hsia R.-C., McClarty G., Rank R.G., Bavoil P.M.,
RA   Fraser C.M.;
RT   "Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC):
RT   examining the role of niche-specific genes in the evolution of the
RT   Chlamydiaceae.";
RL   Nucleic Acids Res. 31:2134-2147(2003).
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; L39892; AAB41348.1; -; Genomic_DNA.
DR   EMBL; AE015925; AAP04832.1; -; Genomic_DNA.
DR   RefSeq; WP_011006053.1; NC_003361.3.
DR   AlphaFoldDB; P52227; -.
DR   SMR; P52227; -.
DR   STRING; 227941.CCA_00080; -.
DR   EnsemblBacteria; AAP04832; AAP04832; CCA_00080.
DR   KEGG; cca:CCA_00080; -.
DR   eggNOG; COG3118; Bacteria.
DR   HOGENOM; CLU_090389_10_4_0; -.
DR   OMA; KIKICKF; -.
DR   OrthoDB; 1630944at2; -.
DR   Proteomes; UP000002193; 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..102
FT                   /note="Thioredoxin"
FT                   /id="PRO_0000120082"
FT   DOMAIN          1..102
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        28..31
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   102 AA;  11159 MW;  F1B57486973A6ED4 CRC64;
     MVKVVSAENF NSFIATGLVL IDFFAEWCGP CKMLTPVLES LEAEVSSVLI GKVNIDDHPA
     PAEQYGVSSI PTLILFKDGK EVDRVVGLKD KDSLIRLINQ HS