ID   DSBI_SALCH              Reviewed;         225 AA.
AC   Q57JR8;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Protein-disulfide oxidoreductase DsbI {ECO:0000255|HAMAP-Rule:MF_01311};
GN   Name=dsbI {ECO:0000255|HAMAP-Rule:MF_01311}; OrderedLocusNames=SCH_3138;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(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. {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; AE017220; AAX67044.1; -; Genomic_DNA.
DR   RefSeq; WP_000345576.1; NC_006905.1.
DR   AlphaFoldDB; Q57JR8; -.
DR   EnsemblBacteria; AAX67044; AAX67044; SCH_3138.
DR   KEGG; sec:SCH_3138; -.
DR   HOGENOM; CLU_090583_1_0_6; -.
DR   OMA; CGYDNPI; -.
DR   Proteomes; UP000000538; 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..225
FT                   /note="Protein-disulfide oxidoreductase DsbI"
FT                   /id="PRO_0000295645"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01311"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01311"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01311"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01311"
FT   DISULFID        56..59
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01311"
FT   DISULFID        128..154
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01311"
SQ   SEQUENCE   225 AA;  25343 MW;  FF0F27561E0DD2CE CRC64;
     MDFIKGLWRD LRARPVDTLV RWQEQRFLWL LMAIAMGGLI ILAHSFFQIY LYMAPCEQCV
     YIRYAMFVMV IGGVIAAINP KNIVLKLIGC IAAFYGSIMG IKFSIKLNGI HHAVHNADPD
     SLFGVQGCST DPTFPFNLPL AEWAPEWFKP TGDCGYDAPI VPDGVTLSSV QQWFVDLYQQ
     SEGWYLLPPW HFMNMAQACM LAFGLCLILL LVMSGAWALK LARGK