DSBI_ECOUT
ID DSBI_ECOUT Reviewed; 223 AA.
AC Q1R6U2;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Protein-disulfide oxidoreductase DsbI {ECO:0000255|HAMAP-Rule:MF_01311};
GN Name=dsbI {ECO:0000255|HAMAP-Rule:MF_01311}; OrderedLocusNames=UTI89_C3475;
OS Escherichia coli (strain UTI89 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=364106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTI89 / UPEC;
RX PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA Gordon J.I.;
RT "Identification of genes subject to positive selection in uropathogenic
RT strains of Escherichia coli: a comparative genomics approach.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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; CP000243; ABE08922.1; -; Genomic_DNA.
DR RefSeq; WP_000511506.1; NC_007946.1.
DR AlphaFoldDB; Q1R6U2; -.
DR EnsemblBacteria; ABE08922; ABE08922; UTI89_C3475.
DR KEGG; eci:UTI89_C3475; -.
DR HOGENOM; CLU_090583_1_0_6; -.
DR OMA; CGYDNPI; -.
DR Proteomes; UP000001952; 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..223
FT /note="Protein-disulfide oxidoreductase DsbI"
FT /id="PRO_0000295642"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01311"
FT TRANSMEM 59..78
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01311"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01311"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01311"
FT DISULFID 55..58
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01311"
FT DISULFID 127..153
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01311"
SQ SEQUENCE 223 AA; 25117 MW; 5DA1DF0D25A11497 CRC64;
MGIKGMWKDL RTSPVDTLVR WQEQRLLWLL MAVAMGALII LAHSFFQIYL YMAPCEQCVY
IRYAMFVMVI GGLVAAINPK NIILKLIGCV MAFYGSILGL KFSLKLNDIH HAVHNPDPDS
LFGVQGCSTD PTFPFNLPLA QWAPNWFKPT GDCGYDAPIV PDGVTLSSTQ QWFVEMYQQS
EGWYLLPPWH FMNMAQACML AFGMCLVLLV IMSGAWALKI IRG
