ID   DSB_RICTY               Reviewed;         270 AA.
AC   Q68XQ3;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Putative protein-disulfide oxidoreductase RT0103;
DE            EC=1.8.-.-;
DE   Flags: Precursor;
GN   OrderedLocusNames=RT0103;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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; AE017197; AAU03589.1; -; Genomic_DNA.
DR   RefSeq; WP_011190576.1; NC_006142.1.
DR   AlphaFoldDB; Q68XQ3; -.
DR   SMR; Q68XQ3; -.
DR   STRING; 257363.RT0103; -.
DR   EnsemblBacteria; AAU03589; AAU03589; RT0103.
DR   KEGG; rty:RT0103; -.
DR   eggNOG; COG1651; Bacteria.
DR   HOGENOM; CLU_1022630_0_0_5; -.
DR   OMA; SACHKTE; -.
DR   OrthoDB; 1678187at2; -.
DR   Proteomes; UP000000604; 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..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..270
FT                   /note="Putative protein-disulfide oxidoreductase RT0103"
FT                   /id="PRO_0000259992"
FT   DOMAIN          71..264
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        117..120
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   270 AA;  30708 MW;  5FAC9AB7B8A9E403 CRC64;
     MKNIFIVLIF LFLSSCAEVK AQDKQHEEQQ IIEQEPLQNN ETPQEANQES INSANTAKSV
     LHNHDNNQTE SVLTQDLHEQ KKTAITTKVT FKIDNNDMVL GNKKSNVIVV EYFSPTCPHC
     AYYHQTIFPA LKKKYIDTNK IAYVVREFIA TKQDLDAAIL ARCKGDINSF IQFHNIILQQ
     QDKWAYSNKY RELLTDIGQL GGISPEEYKQ CLNSDKITET LIANTNLVAK APKFIGTPSF
     FVNGVQTENY SIDNISRAVD RALEDETKSK