ID   DSBI_CAMJR              Reviewed;         266 AA.
AC   Q5HUT1;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Putative protein-disulfide oxidoreductase DsbI;
GN   Name=dsbI; OrderedLocusNames=CJE0952;
OS   Campylobacter jejuni (strain RM1221).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=195099;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM1221;
RX   PubMed=15660156; DOI=10.1371/journal.pbio.0030015;
RA   Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A.,
RA   Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C.,
RA   Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U.,
RA   Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M.,
RA   Nelson K.E.;
RT   "Major structural differences and novel potential virulence mechanisms from
RT   the genomes of multiple Campylobacter species.";
RL   PLoS Biol. 3:72-85(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAW35289.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000025; AAW35289.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_002867468.1; NC_003912.7.
DR   AlphaFoldDB; Q5HUT1; -.
DR   KEGG; cjr:CJE0952; -.
DR   HOGENOM; CLU_090583_0_0_7; -.
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; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..266
FT                   /note="Putative protein-disulfide oxidoreductase DsbI"
FT                   /id="PRO_0000295641"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        226..246
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;  30455 MW;  D94DACC5C03BC5B0 CRC64;
     MSYIKMKDNC RNFSLSKWQD TRKPWLILII VTIGLTCIAH FLFQEYLFMK PCEQCVYIRF
     DMLVMAIGGM IALINPANNI IKIFSYSLAF YGIWLGLEHC LTLNHIHEVV HSENPFAGVD
     GCREIPIYPF NLPLYKWAPS WFLPTGECGM DTPVVPENAY NHLNAFQKFF IGTPPDFENG
     LYSNGWYLIP SLKFMNMAIC CLIAFLCCFV VLFAMFIAYV LDKNKPNAKI FALVIVALVL
     VLKFIGESKN PNQNIASLNQ VVLRYS