ID   DSB_RICFE               Reviewed;         278 AA.
AC   Q4UNH3;
DT   14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Putative protein-disulfide oxidoreductase RF_0032;
DE            EC=1.8.-.-;
DE   Flags: Precursor;
GN   OrderedLocusNames=RF_0032;
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=315456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
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; CP000053; AAY60883.1; -; Genomic_DNA.
DR   RefSeq; WP_011270388.1; NC_007109.1.
DR   AlphaFoldDB; Q4UNH3; -.
DR   SMR; Q4UNH3; -.
DR   STRING; 315456.RF_0032; -.
DR   EnsemblBacteria; AAY60883; AAY60883; RF_0032.
DR   KEGG; rfe:RF_0032; -.
DR   eggNOG; COG1651; Bacteria.
DR   HOGENOM; CLU_1022630_0_0_5; -.
DR   OMA; SACHKTE; -.
DR   OrthoDB; 1678187at2; -.
DR   Proteomes; UP000008548; 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..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..278
FT                   /note="Putative protein-disulfide oxidoreductase RF_0032"
FT                   /id="PRO_0000259990"
FT   DOMAIN          77..266
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          62..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..82
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        119..122
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   278 AA;  31414 MW;  52818097296CCF18 CRC64;
     MRSIFIVPIF LLFLSSCSEE KTQNKNQEEK QIIVQETLQN NNTSQEINQE AVNSENAAES
     IVPANDNNQT DEVSTPPSQE QKNPEIKPVK VTFKVDDNDM VLGNKKSNVI VVEYFSPTCP
     HCAYYHQTIF PELKKKYIDT NKIAYVVREF IATKQDLDAA ILARCKGDIN SFVQFHNIIL
     QQQDKWAYSN KYRELLTDIG QLGGVPPEEY KQCLNSDKIT ETLIANTNFV ANAPKFIGTP
     SFFVNGVQTG NYSIDSISTA VDKALEEQKE KAKNEMSL