(data stored in SCRATCH zone)

SWISSPROT: C5B756_EDWI9

ID   C5B756_EDWI9            Unreviewed;       223 AA.
AC   C5B756;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 47.
DE   RecName: Full=Thiol:disulfide interchange protein DsbL {ECO:0000256|HAMAP-Rule:MF_00932};
DE   Flags: Precursor;
GN   Name=dsbL {ECO:0000256|HAMAP-Rule:MF_00932};
GN   OrderedLocusNames=NT01EI_0601 {ECO:0000313|EMBL:ACR67830.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67830.1, 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.
CC   -!- FUNCTION: Involved in disulfide-bond formation. Acts by
CC       transferring its disulfide bond to other proteins. Part of a redox
CC       system composed of DsbI and DsbL that mediates formation of an
CC       essential disulfide bond in AssT. {ECO:0000256|HAMAP-
CC       Rule:MF_00932}.
CC   -!- SUBUNIT: Interacts with DsbI. {ECO:0000256|HAMAP-Rule:MF_00932}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|HAMAP-Rule:MF_00932}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbL subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00932}.
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DR   EMBL; CP001600; ACR67830.1; -; Genomic_DNA.
DR   RefSeq; WP_015870027.1; NC_012779.2.
DR   ProteinModelPortal; C5B756; -.
DR   STRING; 634503.NT01EI_0601; -.
DR   EnsemblBacteria; ACR67830; ACR67830; NT01EI_0601.
DR   GeneID; 7960369; -.
DR   KEGG; eic:NT01EI_0601; -.
DR   PATRIC; fig|634503.3.peg.545; -.
DR   eggNOG; ENOG4108N92; Bacteria.
DR   eggNOG; COG0526; LUCA.
DR   HOGENOM; HOG000265317; -.
DR   KO; K03673; -.
DR   OMA; YEVAKIQ; -.
DR   OrthoDB; POG091H040A; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:UniProtKB-HAMAP.
DR   CDD; cd03019; DsbA_DsbA; 1.
DR   HAMAP; MF_00932; DsbL; 1.
DR   InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR   InterPro; IPR023205; DsbA/DsbL.
DR   InterPro; IPR028588; DsbL.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   Pfam; PF01323; DSBA; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5B756.
DR   SWISS-2DPAGE; C5B756.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_00932};
KW   Periplasm {ECO:0000256|HAMAP-Rule:MF_00932};
KW   Redox-active center {ECO:0000256|HAMAP-Rule:MF_00932};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_00932}.
FT   SIGNAL        1     27       {ECO:0000256|HAMAP-Rule:MF_00932}.
FT   CHAIN        28    223       Thiol:disulfide interchange protein DsbL.
FT                                {ECO:0000256|HAMAP-Rule:MF_00932}.
FT                                /FTId=PRO_5009008507.
FT   DOMAIN       49    203       DSBA. {ECO:0000259|Pfam:PF01323}.
FT   DISULFID     56     59       Redox-active. {ECO:0000256|HAMAP-Rule:
FT                                MF_00932}.
SQ   SEQUENCE   223 AA;  24368 MW;  B9B114C312583534 CRC64;
     MHLTLGKTHL KALLSATLLT CAFGAAAFSE GTDYVVLEKP IPNAQKTLIK VFSYDCPFCY
     KYDKAVTGPV SEKVKDVVRF EPYHLDTKGV YGPQGSEILA VLLNKDRTAG VSIFDDASQF
     KKAKFAYYAA YHDKKERWKD GKDPAAFTQT GLDAAGLSHA DLEEGLKDPA VQNTLGEWKA
     SAYDVAKIQG VPAYVVNGKY LLMTKSIKSV DSMADLVKEL AAK
//

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