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 27-MAR-2024, entry version 102.
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; Pseudomonadota; 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.gene:17555108; -.
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 OrthoDB; 8478320at2; -.
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 Gene3D; 3.40.30.10; Glutaredoxin; 1.
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; Thioredoxin-like; 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
//
