DSBI_SALTI
ID DSBI_SALTI Reviewed; 225 AA.
AC P0A1H2; Q8XEK0;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Protein-disulfide oxidoreductase DsbI {ECO:0000255|HAMAP-Rule:MF_01311};
GN Name=dsbI {ECO:0000255|HAMAP-Rule:MF_01311};
GN OrderedLocusNames=STY3372, t3114;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD07719.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO70657.1; -; Genomic_DNA.
DR RefSeq; NP_457585.1; NC_003198.1.
DR RefSeq; WP_000345576.1; NZ_WSUR01000003.1.
DR AlphaFoldDB; P0A1H2; -.
DR STRING; 220341.16504271; -.
DR EnsemblBacteria; AAO70657; AAO70657; t3114.
DR KEGG; stt:t3114; -.
DR KEGG; sty:STY3372; -.
DR PATRIC; fig|220341.7.peg.3433; -.
DR eggNOG; COG1495; Bacteria.
DR HOGENOM; CLU_090583_1_0_6; -.
DR OMA; CGYDNPI; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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_0000059390"
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
