ID   DSBI_LELAM              Reviewed;         221 AA.
AC   Q9XDP0;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Protein-disulfide oxidoreductase DsbI {ECO:0000255|HAMAP-Rule:MF_01311};
GN   Name=dsbI {ECO:0000255|HAMAP-Rule:MF_01311};
OS   Lelliottia amnigena (Enterobacter amnigenus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Lelliottia.
OX   NCBI_TaxID=61646;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AR-37;
RX   PubMed=10600454; DOI=10.1006/prep.1999.1129;
RA   Kwon A.-R., Oh T.-G., Kim D.-H., Choi E.-C.;
RT   "Molecular cloning of the arylsulfate sulfotransferase gene and
RT   characterization of its product from Enterobacter amnigenus AR-37.";
RL   Protein Expr. Purif. 17:366-372(1999).
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}.
CC   -!- CAUTION: Has been given the gene name dsbB; however this is a longer
CC       form which is more closely related to the DsbI subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF012826; AAD41462.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9XDP0; -.
DR   BRENDA; 1.8.4.2; 2085.
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..221
FT                   /note="Protein-disulfide oxidoreductase DsbI"
FT                   /id="PRO_0000059389"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01311"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01311"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01311"
FT   TRANSMEM        189..209
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   221 AA;  24492 MW;  E76B64C74C58A2AF CRC64;
     MVDIKGMWKD LRATPVETLV RWQEQRFLWL LMAVAMGGLI ILAHSFFQIY LYMAPCEQCV
     YIRFAMFVMV FGGLIAAINP KNIILKLIGC LAAFYGSIMG IKFSVKLNGI HYAVHNPDPD
     ALFGVQGCST DPTFPFGLPL AEWAPEWFRP TGDCGYDAPV VLTRNAQFCP AVVCGNVSAL
     RRLVSDPALA FYEYGAGVPA GVWAMFCTVA DYERRLGNQA D