ID   DSBC_BORA1              Reviewed;         277 AA.
AC   Q2KU21;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Probable thiol:disulfide interchange protein DsbC;
DE   Flags: Precursor;
GN   Name=dsbC; OrderedLocusNames=BAV3229;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=197N;
RX   PubMed=16885469; DOI=10.1128/jb.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA   Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA   Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA   Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT   with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT   extensive diversity in surface structures associated with host
RT   interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ50839.1; -; Genomic_DNA.
DR   RefSeq; WP_012418866.1; NC_010645.1.
DR   AlphaFoldDB; Q2KU21; -.
DR   SMR; Q2KU21; -.
DR   STRING; 360910.BAV3229; -.
DR   EnsemblBacteria; CAJ50839; CAJ50839; BAV3229.
DR   GeneID; 41395063; -.
DR   KEGG; bav:BAV3229; -.
DR   eggNOG; COG1651; Bacteria.
DR   HOGENOM; CLU_083593_1_0_4; -.
DR   OMA; EINRIKW; -.
DR   OrthoDB; 1678187at2; -.
DR   Proteomes; UP000001977; 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   SUPFAM; SSF54423; SSF54423; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Periplasm; Redox-active center; Reference proteome; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..277
FT                   /note="Probable thiol:disulfide interchange protein DsbC"
FT                   /id="PRO_0000245642"
FT   DISULFID        166..169
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
FT   DISULFID        205..228
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   277 AA;  30568 MW;  CFE1A60C9737C1BD CRC64;
     MKARIIVLLA SLLCANAYAQ NGYSASTAQS SGQNDTVYST NQVGKPATNG GKVYSTTQVQ
     PPDPVTDAVR KRFQLRFQDL KIGVVRPTPY GLFEVQLGGD MFYTDKDVSW VMKGPLIDAA
     TRRDVTRENL EKLSAVSFSE LPLDLAIKQV KGQGKHRIAI FEDPNCGYCK QLRHTLKEMD
     DVTIYTFLYP ILSPDSTVKA RDVLCAADPG KVLDAWMLEG KPPAPAHCRA PIEELVALGE
     KLRVRGTPTL FFEDNTRAAG VLPPAQLRER LTRNVSQ