ID   DSB_RICBR               Reviewed;         259 AA.
AC   Q1RGZ5;
DT   14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Putative protein-disulfide oxidoreductase RBE_1288;
DE            EC=1.8.-.-;
DE   Flags: Precursor;
GN   OrderedLocusNames=RBE_1288;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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}.
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DR   EMBL; CP000087; ABE05369.1; -; Genomic_DNA.
DR   RefSeq; WP_011477939.1; NC_007940.1.
DR   AlphaFoldDB; Q1RGZ5; -.
DR   SMR; Q1RGZ5; -.
DR   STRING; 336407.RBE_1288; -.
DR   EnsemblBacteria; ABE05369; ABE05369; RBE_1288.
DR   KEGG; rbe:RBE_1288; -.
DR   eggNOG; COG1651; Bacteria.
DR   HOGENOM; CLU_1022630_0_0_5; -.
DR   OMA; SACHKTE; -.
DR   OrthoDB; 1678187at2; -.
DR   Proteomes; UP000001951; 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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..259
FT                   /note="Putative protein-disulfide oxidoreductase RBE_1288"
FT                   /id="PRO_0000259989"
FT   DOMAIN          47..251
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          25..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        104..107
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   259 AA;  29178 MW;  2CDE8B088FB49701 CRC64;
     MRNSFITLIF LLLLSGCSEE KEKVVEQESS ESITPAQAST SDENNNQTTE TTTPAVITPA
     VQEQIEQKPE VKTFKVTFKI DENDMVLGNK DSKIVVVEYF SPTCPHCAYY HSTIFPELKQ
     KYIDTNKIAY VTREFIATKQ DLDASILARC KGDINSFMLF HDIILKQQDK WSVSNKYREL
     LTDIGQLGGV TPEEYKKCLS DDKITETLIA NTNFITKAPK FIGTPSFFVN GVQTENYSIN
     SISAAIDKAI EESKNKIDL