ID   DSBI_CAMJE              Reviewed;         266 AA.
AC   Q0PA25; Q46097; Q9PP58;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Putative protein-disulfide oxidoreductase DsbI;
GN   Name=dsbI; OrderedLocusNames=Cj0865;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
CC   -!- FUNCTION: Required for disulfide bond formation in some proteins. Part
CC       of a redox system composed of DsbI and DsbL that mediates formation of
CC       an essential disulfide bond in AssT (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with DsbL. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DsbB family. DsbI subfamily. {ECO:0000305}.
CC   -!- CAUTION: Was originally given the gene name dsbB; however this seems to
CC       belong to a different DsbB subfamily. {ECO:0000305}.
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DR   EMBL; AL111168; CAL34993.1; -; Genomic_DNA.
DR   PIR; A81360; A81360.
DR   RefSeq; WP_002865484.1; NC_002163.1.
DR   RefSeq; YP_002344272.1; NC_002163.1.
DR   AlphaFoldDB; Q0PA25; -.
DR   IntAct; Q0PA25; 19.
DR   STRING; 192222.Cj0865; -.
DR   PaxDb; Q0PA25; -.
DR   EnsemblBacteria; CAL34993; CAL34993; Cj0865.
DR   GeneID; 905166; -.
DR   KEGG; cje:Cj0865; -.
DR   PATRIC; fig|192222.6.peg.853; -.
DR   eggNOG; COG1495; Bacteria.
DR   HOGENOM; CLU_090583_0_0_7; -.
DR   OMA; CGYDNPI; -.
DR   Proteomes; UP000000799; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   Gene3D; 1.20.1550.10; -; 1.
DR   InterPro; IPR003752; DiS_bond_form_DsbB/BdbC.
DR   InterPro; IPR023380; DsbB-like_sf.
DR   Pfam; PF02600; DsbB; 1.
DR   SUPFAM; SSF158442; SSF158442; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Disulfide bond; Electron transport;
KW   Membrane; Oxidoreductase; Redox-active center; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..266
FT                   /note="Putative protein-disulfide oxidoreductase DsbI"
FT                   /id="PRO_0000059387"
FT   TRANSMEM        25..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        62..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        198..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        230..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DISULFID        52..55
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
FT   DISULFID        122..148
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   266 AA;  30399 MW;  55F4BA79E85A34B4 CRC64;
     MSCIKMKDKC RNFSLSKWQD TRKPWLILII VTIGLTCIAH FLFQEYLFMK PCEQCVYIRF
     DMLVMAIGGM IALINPANNI IKIFSYSLAF YGIWLGLEHC LTLNHIHEVV HSENPFAGVD
     GCREIPIYPF NLPLYKWASS WFLPTGECGM DTPVVPENAY NHLNAFQKFF IGTPPDFENG
     LYSNGWYLIP SLKFMNMAIC CLIAFLCCFV VLFAMFIAYV LDKNKPNAKI FALVIVALVL
     VLKFIGESKN PNQNIASLNQ VVLRYS