ID   DSBI_SHEON              Reviewed;         212 AA.
AC   Q8EAM8;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Putative protein-disulfide oxidoreductase DsbI;
GN   Name=dsbI; OrderedLocusNames=SO_3870;
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with DsbL. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DsbB family. DsbI subfamily. {ECO:0000305}.
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DR   EMBL; AE014299; AAN56846.1; -; Genomic_DNA.
DR   RefSeq; NP_719402.1; NC_004347.2.
DR   RefSeq; WP_011073626.1; NZ_CP053946.1.
DR   AlphaFoldDB; Q8EAM8; -.
DR   STRING; 211586.SO_3870; -.
DR   PaxDb; Q8EAM8; -.
DR   KEGG; son:SO_3870; -.
DR   PATRIC; fig|211586.12.peg.3757; -.
DR   eggNOG; COG1495; Bacteria.
DR   HOGENOM; CLU_090583_1_0_6; -.
DR   OMA; CGYDNPI; -.
DR   OrthoDB; 1859420at2; -.
DR   PhylomeDB; Q8EAM8; -.
DR   BioCyc; SONE211586:G1GMP-3591-MON; -.
DR   Proteomes; UP000008186; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   Gene3D; 1.20.1550.10; -; 1.
DR   InterPro; IPR003752; DiS_bond_form_DsbB/BdbC.
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; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..212
FT                   /note="Putative protein-disulfide oxidoreductase DsbI"
FT                   /id="PRO_0000059392"
FT   TRANSMEM        27..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        177..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DISULFID        55..58
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
FT   DISULFID        135..161
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   212 AA;  23895 MW;  D2F625CAB7B8C481 CRC64;
     MSINEVFRSF KAQPVNQLAK IQAERPIWFV MVGAAIFLIL SAIFYFQLFL AMAPCEKCVY
     IRFSQSCIVI AGLIILINPR NNILKTLGLL LAWYAMIQGW IWSFELMKIH DAAHMVVDES
     MDFFAAAGDA AGSACSTEPR FPLGLPLDKW LPFEFAPTGG CGEDDWALFG LNMAHYCMIA
     YATFMVCLAP LTLGWFASFM TDRRNTIVYQ TR