ID   DSBC_BORPE              Reviewed;         279 AA.
AC   Q7VU58;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Probable thiol:disulfide interchange protein DsbC;
DE   Flags: Precursor;
GN   Name=dsbC; OrderedLocusNames=BP3270;
OS   Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257313;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
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).
RN   [2]
RP   FUNCTION IN PERTUSSIS TOXIN SECRETION.
RC   STRAIN=Tohama I / BP338;
RX   PubMed=11953363; DOI=10.1128/iai.70.5.2297-2303.2002;
RA   Stenson T.H., Weiss A.A.;
RT   "DsbA and DsbC are required for secretion of pertussis toxin by Bordetella
RT   pertussis.";
RL   Infect. Immun. 70:2297-2303(2002).
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). Necessary for extracellular
CC       secretion of the pertussis toxin (PTX). {ECO:0000250,
CC       ECO:0000269|PubMed:11953363}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbC subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BX640421; CAE43536.1; -; Genomic_DNA.
DR   RefSeq; NP_881814.1; NC_002929.2.
DR   RefSeq; WP_010931379.1; NZ_CP039022.1.
DR   AlphaFoldDB; Q7VU58; -.
DR   SMR; Q7VU58; -.
DR   STRING; 257313.BP3270; -.
DR   GeneID; 45387624; -.
DR   KEGG; bpe:BP3270; -.
DR   PATRIC; fig|257313.5.peg.3541; -.
DR   eggNOG; COG1651; Bacteria.
DR   HOGENOM; CLU_083593_1_0_4; -.
DR   OMA; QMIVYKA; -.
DR   Proteomes; UP000002676; 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   1: Evidence at protein level;
KW   Disulfide bond; Periplasm; Redox-active center; Reference proteome; Signal.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..279
FT                   /note="Probable thiol:disulfide interchange protein DsbC"
FT                   /id="PRO_0000245645"
FT   REGION          33..73
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;  30659 MW;  A18134861A5F13AD CRC64;
     MSGPSFSGAG MNFRITVWCA AAAVWSSGAL AQDGAGQAAP GTPDKVYSTT GSAPAKPGDK
     VYSTRSAQAP DPQADAVKER FAQRFEGFDV TAVRRTPYGL FEVQIGTDLL YTDEKVTWVM
     EGPLIDALTR RDVTRERQEK LSSVPFEELP LDLAVKQVKG DGSRVMAVFE DPNCGYCKQL
     HRTLEDMDNI TVYTFLYPIL SPDSTTKVRD IWCASDPAKV WKDWMVRGQR PPTAECDAPV
     DQWLALGRQL MVRGTPAIFF KSGGRVSGAL PRDELEARL