ID DSBC_BORBR Reviewed; 279 AA.
AC Q7WEL4;
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=BB4620;
OS Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS (Alcaligenes bronchisepticus).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
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; BX640451; CAE34982.1; -; Genomic_DNA.
DR RefSeq; WP_003815375.1; NC_002927.3.
DR AlphaFoldDB; Q7WEL4; -.
DR SMR; Q7WEL4; -.
DR GeneID; 69423538; -.
DR KEGG; bbr:BB4620; -.
DR eggNOG; COG1651; Bacteria.
DR HOGENOM; CLU_083593_1_0_4; -.
DR Proteomes; UP000001027; 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 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_0000245643"
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
//
