ID   DSBC_BORPA              Reviewed;         279 AA.
AC   Q7W396;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Probable thiol:disulfide interchange protein DsbC;
DE   Flags: Precursor;
GN   Name=dsbC; OrderedLocusNames=BPP4150;
OS   Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
CC   -!- FUNCTION: Required for disulfide bond formation in some periplasmic
CC       proteins. Acts by transferring its disulfide bond to other proteins and
CC       is reduced in the process (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbC subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BX640435; CAE39429.1; -; Genomic_DNA.
DR   RefSeq; WP_003815375.1; NC_002928.3.
DR   AlphaFoldDB; Q7W396; -.
DR   SMR; Q7W396; -.
DR   EnsemblBacteria; CAE39429; CAE39429; BPP4150.
DR   GeneID; 56476881; -.
DR   GeneID; 66440593; -.
DR   KEGG; bpa:BPP4150; -.
DR   HOGENOM; CLU_083593_1_0_4; -.
DR   OMA; QMIVYKA; -.
DR   Proteomes; UP000001421; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   CDD; cd03020; DsbA_DsbC_DsbG; 1.
DR   Gene3D; 3.10.450.70; -; 1.
DR   InterPro; IPR033954; DiS-bond_Isoase_DsbC/G.
DR   InterPro; IPR018950; DiS-bond_isomerase_DsbC/G_N.
DR   InterPro; IPR009094; DiS-bond_isomerase_DsbC/G_N_sf.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   Pfam; PF10411; DsbC_N; 1.
DR   Pfam; PF13098; Thioredoxin_2; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Periplasm; Redox-active center; Signal.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..279
FT                   /note="Probable thiol:disulfide interchange protein DsbC"
FT                   /id="PRO_0000245644"
FT   REGION          33..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        174..177
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
FT   DISULFID        213..236
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   279 AA;  30683 MW;  367CD6DC9DDCCDD1 CRC64;
     MSGPPFSGAG MNFRITVWCA AAAVWSSGAL AQDGAGQAAP GTPDKVYSTT GTAPAKPGDK
     VYSTRSAQAP DPQADAVKER FAQRFEGFDV TAVRRTPYGL FEVQIGTDLL YTDEKVTWVM
     EGPLIDALTR RDVTRERQEK LSSVPFDELP LDLAVKQVKG DGSRVMAVFE DPNCGYCKQL
     HRTLEDMDNI TVYTFLYPIL SPDSTTKVRD IWCASDPAKV WKDWMVRGQR PPTAECDAPV
     EQWLALGRQL MVRGTPAIFF KSGGRVSGAL PRDELEARL