ID   DSBI_ECOK1              Reviewed;         223 AA.
AC   A1AFW3;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Protein-disulfide oxidoreductase DsbI {ECO:0000255|HAMAP-Rule:MF_01311};
GN   Name=dsbI {ECO:0000255|HAMAP-Rule:MF_01311}; OrderedLocusNames=Ecok1_30590;
GN   ORFNames=APECO1_3373;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17293413; DOI=10.1128/jb.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA   Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT   shares strong similarities with human extraintestinal pathogenic E. coli
RT   genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
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   -!- SUBUNIT: Interacts with DsbL. {ECO:0000255|HAMAP-Rule:MF_01311}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01311}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01311}.
CC   -!- SIMILARITY: Belongs to the DsbB family. DsbI subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01311}.
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DR   EMBL; CP000468; ABJ02553.1; -; Genomic_DNA.
DR   RefSeq; WP_000511506.1; NC_008563.1.
DR   AlphaFoldDB; A1AFW3; -.
DR   EnsemblBacteria; ABJ02553; ABJ02553; APECO1_3373.
DR   KEGG; ecv:APECO1_3373; -.
DR   HOGENOM; CLU_090583_1_0_6; -.
DR   OMA; CGYDNPI; -.
DR   Proteomes; UP000008216; 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   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..223
FT                   /note="Protein-disulfide oxidoreductase DsbI"
FT                   /id="PRO_0000295643"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01311"
FT   TRANSMEM        59..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01311"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01311"
FT   TRANSMEM        198..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01311"
FT   DISULFID        55..58
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01311"
FT   DISULFID        127..153
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01311"
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