ID   DSB_RICPR               Reviewed;         272 AA.
AC   Q9ZEB9;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Putative protein-disulfide oxidoreductase RP025;
DE            EC=1.8.-.-;
DE   Flags: Precursor;
GN   OrderedLocusNames=RP025;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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; AJ235270; CAA14496.1; -; Genomic_DNA.
DR   PIR; A71710; A71710.
DR   RefSeq; NP_220419.1; NC_000963.1.
DR   RefSeq; WP_004596665.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZEB9; -.
DR   SMR; Q9ZEB9; -.
DR   STRING; 272947.RP025; -.
DR   EnsemblBacteria; CAA14496; CAA14496; CAA14496.
DR   GeneID; 57569154; -.
DR   KEGG; rpr:RP025; -.
DR   PATRIC; fig|272947.5.peg.25; -.
DR   eggNOG; COG1651; Bacteria.
DR   HOGENOM; CLU_1022630_0_0_5; -.
DR   OMA; SACHKTE; -.
DR   Proteomes; UP000002480; 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;
KW   Reference proteome; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..272
FT                   /note="Putative protein-disulfide oxidoreductase RP025"
FT                   /id="PRO_0000259991"
FT   DOMAIN          74..263
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        116..119
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   272 AA;  31142 MW;  97FA84184D217E6D CRC64;
     MRNIFIVLIF LFLSNCSEVK AQDKKYEGKQ IIVQEPLQNN KTPQETNQES INSATKSVVH
     NNDNNQTEEV LIHDSREQKK PEIRPTKVTF KIDDNDMVLG NKKSNVIVVE YFSPTCPHCA
     YYHQTIFPEL KKKYIDTNKI AYVIREFIAT KQDLDAAILA RCKGDINSFI QFHNIILQQQ
     DKWAYSNKYR ELLTDIGQLG GIPPEEYKQC LNSDKITATL IANTNLVAKA PKFIGTPSFF
     VNGVQTENYS IDNISKAVDK ALDDETKKQI NF