ID   DSB_RICCN               Reviewed;         277 AA.
AC   Q92JN8;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Putative protein-disulfide oxidoreductase RC0029;
DE            EC=1.8.-.-;
DE   Flags: Precursor;
GN   OrderedLocusNames=RC0029;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
CC   -!- FUNCTION: May be required for disulfide bond formation in some
CC       proteins. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE006914; AAL02567.1; -; Genomic_DNA.
DR   PIR; E97703; E97703.
DR   RefSeq; WP_010976717.1; NC_003103.1.
DR   AlphaFoldDB; Q92JN8; -.
DR   SMR; Q92JN8; -.
DR   EnsemblBacteria; AAL02567; AAL02567; RC0029.
DR   KEGG; rco:RC0029; -.
DR   PATRIC; fig|272944.4.peg.36; -.
DR   HOGENOM; CLU_1022630_0_0_5; -.
DR   OMA; SACHKTE; -.
DR   Proteomes; UP000000816; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF13462; Thioredoxin_4; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Oxidoreductase; Periplasm; Redox-active center; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..277
FT                   /note="Putative protein-disulfide oxidoreductase RC0029"
FT                   /id="PRO_0000259988"
FT   DOMAIN          76..265
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          34..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        118..121
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   277 AA;  31198 MW;  83D5B0D06908CBD7 CRC64;
     MRSIFIILIF LLFLSSCSEE KAQDKNHEEK QIIEHETQNN ETSKATNQEA VNSENTTESI
     VPANDNNQTD EVSTPASQKQ KNPAIKAVKV TFKVDDNDMV LGNKKSNVIV VEYFSPTCPH
     CAYYHQTIFP ELKKKYIDTN KIAYVVREFI ATKQDLDAAI LARCKGDTNS FTQLHNIILI
     QQDKWAYSNK YRELLTDIGQ LGGISPEEYK QCLNNDKITA ILIANTNFVA KAPQFIGTPS
     FFVNGVQTGN YSIDTISTAV DKALEEQKEK AKNEMSL