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 27-MAR-2024, entry version 99.
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; Pseudomonadota; 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}.
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; 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 PaxDb; 257313-BP3270; -.
DR GeneID; 69603196; -.
DR KEGG; bpe:BP3270; -.
DR PATRIC; fig|257313.5.peg.3541; -.
DR eggNOG; COG1651; Bacteria.
DR HOGENOM; CLU_083593_1_0_4; -.
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; Disulphide bond isomerase, DsbC/G, N-terminal; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 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 PANTHER; PTHR35272:SF3; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC; 1.
DR PANTHER; PTHR35272; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC-RELATED; 1.
DR Pfam; PF10411; DsbC_N; 1.
DR Pfam; PF13098; Thioredoxin_2; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 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
//
