ID   DSBI_SALPA              Reviewed;         225 AA.
AC   Q5PMU6;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Protein-disulfide oxidoreductase DsbI {ECO:0000255|HAMAP-Rule:MF_01311};
GN   Name=dsbI {ECO:0000255|HAMAP-Rule:MF_01311}; OrderedLocusNames=SPA3062;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV78897.1; -; Genomic_DNA.
DR   RefSeq; WP_000345576.1; NC_006511.1.
DR   AlphaFoldDB; Q5PMU6; -.
DR   EnsemblBacteria; AAV78897; AAV78897; SPA3062.
DR   KEGG; spt:SPA3062; -.
DR   HOGENOM; CLU_090583_1_0_6; -.
DR   OMA; CGYDNPI; -.
DR   Proteomes; UP000008185; 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_0000295646"
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