ID   DSBI_ECOL6              Reviewed;         223 AA.
AC   Q8FDI3;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Protein-disulfide oxidoreductase DsbI {ECO:0000255|HAMAP-Rule:MF_01311};
GN   Name=dsbI {ECO:0000255|HAMAP-Rule:MF_01311}; OrderedLocusNames=c3787;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
RN   [2]
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-55 AND CYS-58,
RP   AND INDUCTION.
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=18565543; DOI=10.1016/j.jmb.2008.05.031;
RA   Grimshaw J.P., Stirnimann C.U., Brozzo M.S., Malojcic G., Grutter M.G.,
RA   Capitani G., Glockshuber R.;
RT   "DsbL and DsbI form a specific dithiol oxidase system for periplasmic
RT   arylsulfate sulfotransferase in uropathogenic Escherichia coli.";
RL   J. Mol. Biol. 380:667-680(2008).
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. {ECO:0000255|HAMAP-Rule:MF_01311,
CC       ECO:0000269|PubMed:18565543}.
CC   -!- SUBUNIT: Interacts with DsbL. {ECO:0000255|HAMAP-Rule:MF_01311,
CC       ECO:0000269|PubMed:18565543}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000305|PubMed:18565543}; Multi-pass membrane protein
CC       {ECO:0000305|PubMed:18565543}.
CC   -!- INDUCTION: Expressed from a tri-cistronic operon that encodes AssT,
CC       DsbI and DsbL. {ECO:0000269|PubMed:18565543}.
CC   -!- SIMILARITY: Belongs to the DsbB family. DsbI subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01311}.
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DR   EMBL; AE014075; AAN82231.1; -; Genomic_DNA.
DR   RefSeq; WP_000511506.1; NC_004431.1.
DR   AlphaFoldDB; Q8FDI3; -.
DR   STRING; 199310.c3787; -.
DR   TCDB; 5.A.2.1.2; the disulfide bond oxidoreductase b (dsbb) family.
DR   EnsemblBacteria; AAN82231; AAN82231; c3787.
DR   KEGG; ecc:c3787; -.
DR   eggNOG; COG1495; Bacteria.
DR   HOGENOM; CLU_090583_1_0_6; -.
DR   OMA; CGYDNPI; -.
DR   BioCyc; ECOL199310:C3787-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   Gene3D; 1.20.1550.10; -; 1.
DR   HAMAP; MF_01311; DsbI; 1.
DR   InterPro; IPR003752; DiS_bond_form_DsbB/BdbC.
DR   InterPro; IPR023792; DiS_OxRdtase_Dsbl.
DR   InterPro; IPR023380; DsbB-like_sf.
DR   Pfam; PF02600; DsbB; 1.
DR   SUPFAM; SSF158442; SSF158442; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Disulfide bond; Electron transport;
KW   Membrane; Oxidoreductase; Redox-active center; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..223
FT                   /note="Protein-disulfide oxidoreductase DsbI"
FT                   /id="PRO_0000059388"
FT   TOPO_DOM        1..25
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01311"
FT   TOPO_DOM        47..57
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01311"
FT   TOPO_DOM        79..81
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01311"
FT   TOPO_DOM        103..197
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        198..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01311"
FT   TOPO_DOM        219..223
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DISULFID        55..58
FT                   /note="Redox-active"
FT   DISULFID        127..153
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01311"
FT   MUTAGEN         55
FT                   /note="C->S: Loss of activity; when associated with S-58."
FT                   /evidence="ECO:0000269|PubMed:18565543"
FT   MUTAGEN         58
FT                   /note="C->S: Loss of activity; when associated with S-55."
FT                   /evidence="ECO:0000269|PubMed:18565543"
SQ   SEQUENCE   223 AA;  25117 MW;  5DA1DF0D25A11497 CRC64;
     MGIKGMWKDL RTSPVDTLVR WQEQRLLWLL MAVAMGALII LAHSFFQIYL YMAPCEQCVY
     IRYAMFVMVI GGLVAAINPK NIILKLIGCV MAFYGSILGL KFSLKLNDIH HAVHNPDPDS
     LFGVQGCSTD PTFPFNLPLA QWAPNWFKPT GDCGYDAPIV PDGVTLSSTQ QWFVEMYQQS
     EGWYLLPPWH FMNMAQACML AFGMCLVLLV IMSGAWALKI IRG