(data stored in ACNUC7421 zone)

SWISSPROT: C5B755_EDWI9

ID   C5B755_EDWI9            Unreviewed;       233 AA.
AC   C5B755;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 66.
DE   RecName: Full=Protein-disulfide oxidoreductase DsbI {ECO:0000256|HAMAP-Rule:MF_01311};
GN   Name=dsbI {ECO:0000256|HAMAP-Rule:MF_01311};
GN   OrderedLocusNames=NT01EI_0600 {ECO:0000313|EMBL:ACR67829.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67829.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACR67829.1, ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|EMBL:ACR67829.1,
RC   ECO:0000313|Proteomes:UP000001485};
RX   PubMed=22247535; DOI=10.1128/JB.06522-11;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Banes M.M.,
RA   Lawrence M.L.;
RT   "Genome Sequence of Edwardsiella ictaluri 93-146, a Strain Associated
RT   with a Natural Channel Catfish Outbreak of Enteric Septicemia of
RT   Catfish.";
RL   J. Bacteriol. 194:740-741(2012).
CC   -!- FUNCTION: Required for disulfide bond formation in some proteins.
CC       Part of a redox system composed of DsbI and DsbL that mediates
CC       formation of an essential disulfide bond in AssT.
CC       {ECO:0000256|HAMAP-Rule:MF_01311}.
CC   -!- SUBUNIT: Interacts with DsbL. {ECO:0000256|HAMAP-Rule:MF_01311}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01311, ECO:0000256|SAAS:SAAS00726109}; Multi-pass membrane
CC       protein {ECO:0000256|HAMAP-Rule:MF_01311,
CC       ECO:0000256|SAAS:SAAS00726109}.
CC   -!- SIMILARITY: Belongs to the DsbB family. DsbI subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01311}.
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DR   EMBL; CP001600; ACR67829.1; -; Genomic_DNA.
DR   RefSeq; WP_015870026.1; NC_012779.2.
DR   EnsemblBacteria; ACR67829; ACR67829; NT01EI_0600.
DR   GeneID; 7960368; -.
DR   KEGG; eic:NT01EI_0600; -.
DR   PATRIC; fig|634503.3.peg.544; -.
DR   eggNOG; ENOG4108PSN; Bacteria.
DR   eggNOG; COG1495; LUCA.
DR   HOGENOM; HOG000252211; -.
DR   KO; K03611; -.
DR   OMA; CGYDNPI; -.
DR   OrthoDB; 1859420at2; -.
DR   BioCyc; EICT634503:G1GVC-560-MONOMER; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:UniProtKB-UniRule.
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;
DR   PRODOM; C5B755.
DR   SWISS-2DPAGE; C5B755.
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01311,
KW   ECO:0000256|SAAS:SAAS00726201};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01311,
KW   ECO:0000256|SAAS:SAAS00726243};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_01311,
KW   ECO:0000256|SAAS:SAAS00726159};
KW   Electron transport {ECO:0000256|HAMAP-Rule:MF_01311,
KW   ECO:0000256|SAAS:SAAS00726149};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01311,
KW   ECO:0000256|SAAS:SAAS00726177};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01311,
KW   ECO:0000256|SAAS:SAAS00726211};
KW   Redox-active center {ECO:0000256|HAMAP-Rule:MF_01311,
KW   ECO:0000256|SAAS:SAAS00726278};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01311,
KW   ECO:0000256|SAAS:SAAS00726122};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01311,
KW   ECO:0000256|SAAS:SAAS00726187};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01311,
KW   ECO:0000256|SAAS:SAAS00726172}.
FT   TRANSMEM     25     51       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01311}.
FT   TRANSMEM     58     76       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01311}.
FT   TRANSMEM     82    103       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01311}.
FT   TRANSMEM    194    215       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01311}.
FT   DISULFID     54     57       Redox-active. {ECO:0000256|HAMAP-Rule:
FT                                MF_01311}.
FT   DISULFID    124    150       Redox-active. {ECO:0000256|HAMAP-Rule:
FT                                MF_01311}.
SQ   SEQUENCE   233 AA;  26104 MW;  48EA6934E92004D5 CRC64;
     MSAKMWSDLR QNPVETLVRW QERRFLWLLM ALAMGGLIVL AHAFFQIYLY MAPCEQCVYI
     RFAMFVMVIG GLVAAINPRN LALKLFGCIA AFYGAIIGMG YSIKLNGIHH AVHSPDALFG
     VQGCSTDPHF PFGLPLAEWS PSWFKPTGDC GYDAPMVPQG VALDSVQQWF IDMYVQAEGW
     YLIPSMQFMN MAQACFLAFA LCFAILVIMS VAWAIHLLRR RAVPADHTAS TPR
//

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